Phage-Borne Depolymerases Decrease Klebsiella pneumoniae Resistance to Innate Defense Mechanisms (374 views)
Front Microbiol (ISSN: 1664-302xprint, 1664-302xlinking, 1664-302xelectronic), 2018 Oct 23; 9(OCT): 2517-2517.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 4.076, 5-year impact factor: 4.526
Url: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85055849009&doi=10.3389%2ffmicb.2018.02517&partnerID=40&md5=6fab09084e11aa36171d9b1bcb593160
Keywords: Klebsiella Sp, Bacteriophage, Capsule, Innate Immunity, Polysaccharide Depolymerase,
Affiliations:
*** IBB - CNR ***
Department of Pathogen Biology and Immunology, Institute of Genetics and Microbiology, University of Wroclaw, Wroclaw, Poland., Laboratory of Applied Biotechnology, Department of Biotechnology, Ghent University, Ghent, Belgium., Institute of Biostructure and Bioimaging, Italian National Research Council, Naples, Italy.,
References:
Albertí, S., Alvares, D., Merino, S., Casado, M.T., Vivanco, F., Tomas, J.M., Analysis of complement C3 deposition and degradation on Klebsiella pneumoniae (1996) Infect. Immun, 64, pp. 4726-473
Albertí, S., Marqués, G., Camprubí, S., Merino, S., Tomás, J.M., Vivanco, F., C1q binding and activation of the complement classical pathway by Klebsiella pneumoniae outer membrane proteins (1993) Infect. Immun, 61, pp. 852-860
Álvarez, D., Merino, S., Tomás, J.M., Vicente, J., Toma, J.M., Benedi, V.J., Capsular polysaccharide is a major complement resistance factor in lipopolysaccharide o side chain-deficient Klebsiella pneumoniae clinical isolates (2000) Infect. Immun., 68, pp. 953-955
Athamna, A., Ofek, I., Keisari, Y., Markowitz, S., Dutton, G.G.S., Sharon, N., Lectinophagocytosis of encapsulated Klebsiella pneumoniae mediated by surface lectins of Guinea-pig alveolar macrophages and human monocyte-derived macrophages (1991) Infect. Immun, 59, pp. 1673-1682
Augustyniak, D., Jankowski, A., Mackiewicz, P., Skowyra, A., Gutowicz, J., Drulis-Kawa, Z., Innate immune properties of selected human neuropeptides against Moraxella catarrhalis and nontypeable Haemophilus influenzae (2012) BMC Immunol., 13, p. 24
Augustyniak, D., Piekut, M., Majkowska-Skrobek, G., Skala, J., Bactericidal, opsonophagocytic and anti-adhesive effectiveness of cross-reactive antibodies against Moraxella catarrhalis (2015) Pathog. Dis., 73, p. ftu026
Bansal, S., Harjai, K., Chhibber, S., Depolymerase improves gentamicin efficacy during Klebsiella pneumoniae induced murine infection (2014) BMC Infect. Dis., 14, p. 456
Barbirz, S., Müller, J.J., Uetrecht, C., Clark, A.J., Heinemann, U., Seckler, R., Crystal structure of Escherichia coli phage HK620 tailspike: Podoviral tailspike endoglycosidase modules are evolutionarily related (2008) Mol. Microbiol., 69, pp. 303-316
Bessler, W., Freund-Mölbert, E., Knüfermann, H., Rudolph, C., Thurow, H., Stirm, S., A bacteriophage-induced depolymerase active on Klebsiella K11 capsular polysaccharide (1973) Virology, 56, pp. 134-151
Blumenkrantz, N., Asboe-Hansen, G., New method for quantitative determination of uronic acids (1973) Anal. Biochem, 54, pp. 484-489
Brisse, S., Passet, V., Haugaard, A.B., Babosan, A., Kassis-Chikhani, N., Struve, C., Wzi gene sequencing, a rapid method for determination of capsulartype for Klebsiella strains (2013) J. Clin. Microbiol., 51, pp. 4073-4078
Cortés, G., Borrell, N., De Astorza, B., Gómez, C., Sauleda, J., Albertí, S., Molecular analysis of the contribution of the capsular polysaccharide and the lipopolysaccharide O side chain to the virulence of Klebsiella pneumoniae in a murine model of pneumonia (2002) Infect. Immun, 70, pp. 2583-2590
Cryz, S.J., Mortimer, P.M., Mansfield, V., Germanier, R., Seroepidemiology of Klebsiella bacteremic isolates and implications for vaccine development (1986) J. Clin. Microbiol., 23, pp. 687-690
Domenico, P., Diedrich, D.L., Cunha, B.A., Quantitative extraction and purification of exopolysaccharides from Klebsiella pneumoniae (1989) J. Microbiol. Methods, 9, pp. 211-219
Doorduijn, D.J., Rooijakkers, S.H.M., Van Schaik, W., Bardoel, B.W., Complement resistance mechanisms of Klebsiella pneumoniae (2016) Immunobiology, 221, pp. 1102-1109
Drulis-Kawa, Z., Majkowska-Skrobek, G., Maciejewska, B., Bacteriophages and phagederived proteins - Application approaches (2015) Curr. Med. Chem, 22, pp. 1757-1773
Dutton, G.G.S., Choy, Y.M., Capsular polysaccharide from Klebsiella type 21 (1972) Carbohydr. Res., 21, pp. 169-172
Dutton, G.G.S., Parolis, H., Joseleau, J.-P., Marais, M.-F., The use of bacteriophage depolymerization in the structural investigation of the capsular polysaccharide from Klebsiella serotype K3 (1986) Carbohydr. Res., 149, pp. 411-423
Hsieh, P.F., Lin, H.H., Lin, T.L., Chen, Y.Y., Wang, J.T., Two T7-like bacteriophages, K5-2 and K5-4, each encodes two capsule depolymerases: Isolation and functional characterization (2017) Sci. Rep, 7, pp. 1-13
Insua, J.L., Llobet, E., Moranta, D., Pérez-Gutiérrez, C., Tomás, A., Garmendia, J., Modeling Klebsiella pneumoniae pathogenesis by infection of the wax moth Galleria mellonella (2013) Infect. Immun, 81, pp. 3552-3565
Kanamaru, S., Leiman, P.G., Kostyuchenko, V.A., Chipman, P.R., Mesyanzhinov, V.V., Arisaka, F., Structure of the cell-puncturing device of bacteriophage T4 (2002) Nature, 415, pp. 553-557
Kassa, T., Chhibber, S., Thermal treatment of the bacteriophage lysate of Klebsiella pneumoniae B5055 as a step for the purification of capsular depolymerase enzyme (2012) J. Virol. Methods, 179, pp. 135-141
Ksik-Szeloch, A., Drulis-Kawa, Z., Weber-Dabrowska, B., Kassner, J., Majkowska-Skrobek, G., Augustyniak, D., Characterising the biology of novel lytic bacteriophages infecting multidrug resistant Klebsiella pneumoniae (2013) Virol. J, 10, pp. 1-12
Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
Latka, A., Maciejewska, B., Majkowska-Skrobek, G., Briers, Y., Drulis-Kawa, Z., Bacteriophage-encoded virion-associated enzymes to overcome the carbohydrate barriers during the infection process (2017) Appl. Microbiol. Biotechnol., 101, pp. 3103-3119
Lawlor, M.S., Hsu, J., Rick, P.D., Miller, V.L., Identification of Klebsiella pneumoniae virulence determinants using an intranasal infection model (2005) Mol. Microbiol., 58, pp. 1054-1073
Leiman, P.G., Molineux, I.J., Evolution of a new enzyme activity from the same motif fold (2008) Mol. Microbiol., 69, pp. 287-290
Li, X.Y., Lin, Z.Y., Zhu, P.P., Jin, Y.F., Effect of cyclophosphamide on serum complement in mice (1987) Zhongguo Yao Li Xue Bao, 8, pp. 79-83
Lin, T.L., Hsieh, P.F., Huang, Y.T., Lee, W.C., Tsai, Y.T., Su, P.A., Isolation of a bacteriophage and its depolymerase specific for K1 capsule of Klebsiella pneumoniae: Implication in typing and treatment (2014) J. Infect. Dis., 210, pp. 1734-1744
Maciejewska, B., Olszak, T., Drulis-Kawa, Z., Applications of bacteriophages versus phage enzymes to combat and cure bacterial infections: An ambitious and also a realistic application? (2018) Appl. Microbiol. Biotechnol., 102, pp. 2563-2581
March, C., Cano, V., Moranta, D., Llobet, E., Pérez-Gutiérrez, C., Tomás, J.M., Role of bacterial surface structures on the interaction of Klebsiella pneumoniae with phagocytes (2013) PLoS One, 8
Martin, R.M., Bachman, M.A., Colonization, infection, and the accessory genome of Klebsiella pneumoniae (2018) Front. Cell. Infect. Microbiol., 8, p. 4
Merino, S., Camprubi, S., Alberti, S., Benedi, V.J., Tomas, J.M., Mechanisms of Klebsiella pneumoniae resistance to complement-mediated killing (1992) Infect. Immun, 60, pp. 2529-2535
Nassif, X., Sansonetti, P.J., Correlation of the virulence of Klebsiella pneumoniae K1 and K2 with the presence of a plasmid encoding aerobactin (1986) Infect. Immun, 54, pp. 603-608
Olszak, T., Shneider, M.M., Latka, A., Maciejewska, B., Browning, C., Sycheva, L.V., The O-specific polysaccharide lyase from the phage LKA1 tailspike reduces Pseudomonas virulence (2017) Sci. Rep, 7, pp. 1-14
Paczosa, M.K., Mecsas, J., Klebsiella pneumoniae: Going on the offense with a strong defense (2016) Microbiol. Mol. Biol. Rev., 80, pp. 629-661
Pan, Y., Lin, T., Chen, C., Tsai, Y., Klebsiella phage FK64-1 encodes multiple depolymerases for multiple host capsular types (2017) J. Virol., 91
Pan, Y.J., Lin, T.L., Chen, Y.H., Hsu, C.R., Hsieh, P.F., Wu, M.C., Capsular types of Klebsiella pneumoniae revisited by wzc sequencing (2013) PLoS One, 8
Podschun, R., Ullmann, U., Klebsiella spp. as nosocomial pathogens: Epidemiology, taxonomy, typing methods, and pathogenicity factors (1998) Clin. Microbiol. Rev., 11, pp. 589-603
Regueiro, V., Campos, M.A., Pons, J., Albertí, S., Bengoechea, J.A., The uptake of a Klebsiella pneumoniae capsule polysaccharide mutant triggers an inflammatory response by human airway epithelial cells (2006) Microbiology, 152, pp. 555-566
Sahly, H., Keisari, Y., Crouch, E., Sharon, N., Ofek, I., Recognition of bacterial surface polysaccharides by lectins of the innate immune system and its contribution to defense against infection: The case of pulmonary pathogens (2008) Infect. Immun, 76, pp. 1322-1332
Shepherd, V.L., Campbell, E.J., Senior, R.M., Stahl, P.D., Characterization of the mannose/fucose receptor on human mononuclear phagocytes (1982) J. Reticuloendothel. Soc, 32, pp. 423-431
Simpson, D.J., Sacher, J.C., Szymanski, C.M., Exploring the interactions between bacteriophage-encoded glycan binding proteins and carbohydrates (2015) Curr. Opin. Struct. Biol., 34, pp. 69-77
Solovieva, E.V., Myakinina, V.P., Kislichkina, A.A., Krasilnikova, V.M., Verevkin, V.V., Mochalov, V.V., Comparative genome analysis of novel Podoviruses lytic for hypermucoviscous Klebsiella pneumoniae of K1. K2, and K57 capsular types (2018) Virus Res., 243, pp. 10-18
Steinbacher, S., Seckler, R., Miller, S., Steipe, B., Huber, R., Reinemer, P., Crystal structure of P22 tailspike protein: Interdigitated subunits in a thermostable trimer (1994) Science, 265, pp. 383-386
Weigele, P.R., Scanlon, E., King, J., Homotrimeric, β-stranded viral adhesins and tail proteins (2003) J. Bacteriol., 185, pp. 4022-4030
Wileman, T.E., Lennartz, M.R., Stahl, P.D., Identification of the macrophage mannose receptor as a 175-kDa membrane protein (1986) Proc. Natl. Acad. Sci. U. S. A., 83, pp. 2501-2505
Wyres, K.L., Wick, R.R., Gorrie, C., Jenney, A., Follador, R., Thomson, N.R., Identification of Klebsiella capsule synthesis loci from whole genome data (2016) Microb. Genomics, 2, pp. 1-15
Yoshida, K., Matsumoto, T., Tateda, K., Uchida, K., Tsujimoto, S., Yamaguchi, K., Role of bacterial capsule in local and systemic inflammatory responses of mice during pulmonary infection with Klebsiella pneumoniae (2000) J. Med. Microbiol., 49, pp. 1003-1010
Front Microbiol (ISSN: 1664-302xprint, 1664-302xlinking, 1664-302xelectronic), 2018 Oct 23; 9(OCT): 2517-2517.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 4.076, 5-year impact factor: 4.526
Url: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85055849009&doi=10.3389%2ffmicb.2018.02517&partnerID=40&md5=6fab09084e11aa36171d9b1bcb593160
Keywords: Klebsiella Sp, Bacteriophage, Capsule, Innate Immunity, Polysaccharide Depolymerase,
Affiliations:
*** IBB - CNR ***
Department of Pathogen Biology and Immunology, Institute of Genetics and Microbiology, University of Wroclaw, Wroclaw, Poland., Laboratory of Applied Biotechnology, Department of Biotechnology, Ghent University, Ghent, Belgium., Institute of Biostructure and Bioimaging, Italian National Research Council, Naples, Italy.,
References:
Albertí, S., Alvares, D., Merino, S., Casado, M.T., Vivanco, F., Tomas, J.M., Analysis of complement C3 deposition and degradation on Klebsiella pneumoniae (1996) Infect. Immun, 64, pp. 4726-473
Albertí, S., Marqués, G., Camprubí, S., Merino, S., Tomás, J.M., Vivanco, F., C1q binding and activation of the complement classical pathway by Klebsiella pneumoniae outer membrane proteins (1993) Infect. Immun, 61, pp. 852-860
Álvarez, D., Merino, S., Tomás, J.M., Vicente, J., Toma, J.M., Benedi, V.J., Capsular polysaccharide is a major complement resistance factor in lipopolysaccharide o side chain-deficient Klebsiella pneumoniae clinical isolates (2000) Infect. Immun., 68, pp. 953-955
Athamna, A., Ofek, I., Keisari, Y., Markowitz, S., Dutton, G.G.S., Sharon, N., Lectinophagocytosis of encapsulated Klebsiella pneumoniae mediated by surface lectins of Guinea-pig alveolar macrophages and human monocyte-derived macrophages (1991) Infect. Immun, 59, pp. 1673-1682
Augustyniak, D., Jankowski, A., Mackiewicz, P., Skowyra, A., Gutowicz, J., Drulis-Kawa, Z., Innate immune properties of selected human neuropeptides against Moraxella catarrhalis and nontypeable Haemophilus influenzae (2012) BMC Immunol., 13, p. 24
Augustyniak, D., Piekut, M., Majkowska-Skrobek, G., Skala, J., Bactericidal, opsonophagocytic and anti-adhesive effectiveness of cross-reactive antibodies against Moraxella catarrhalis (2015) Pathog. Dis., 73, p. ftu026
Bansal, S., Harjai, K., Chhibber, S., Depolymerase improves gentamicin efficacy during Klebsiella pneumoniae induced murine infection (2014) BMC Infect. Dis., 14, p. 456
Barbirz, S., Müller, J.J., Uetrecht, C., Clark, A.J., Heinemann, U., Seckler, R., Crystal structure of Escherichia coli phage HK620 tailspike: Podoviral tailspike endoglycosidase modules are evolutionarily related (2008) Mol. Microbiol., 69, pp. 303-316
Bessler, W., Freund-Mölbert, E., Knüfermann, H., Rudolph, C., Thurow, H., Stirm, S., A bacteriophage-induced depolymerase active on Klebsiella K11 capsular polysaccharide (1973) Virology, 56, pp. 134-151
Blumenkrantz, N., Asboe-Hansen, G., New method for quantitative determination of uronic acids (1973) Anal. Biochem, 54, pp. 484-489
Brisse, S., Passet, V., Haugaard, A.B., Babosan, A., Kassis-Chikhani, N., Struve, C., Wzi gene sequencing, a rapid method for determination of capsulartype for Klebsiella strains (2013) J. Clin. Microbiol., 51, pp. 4073-4078
Cortés, G., Borrell, N., De Astorza, B., Gómez, C., Sauleda, J., Albertí, S., Molecular analysis of the contribution of the capsular polysaccharide and the lipopolysaccharide O side chain to the virulence of Klebsiella pneumoniae in a murine model of pneumonia (2002) Infect. Immun, 70, pp. 2583-2590
Cryz, S.J., Mortimer, P.M., Mansfield, V., Germanier, R., Seroepidemiology of Klebsiella bacteremic isolates and implications for vaccine development (1986) J. Clin. Microbiol., 23, pp. 687-690
Domenico, P., Diedrich, D.L., Cunha, B.A., Quantitative extraction and purification of exopolysaccharides from Klebsiella pneumoniae (1989) J. Microbiol. Methods, 9, pp. 211-219
Doorduijn, D.J., Rooijakkers, S.H.M., Van Schaik, W., Bardoel, B.W., Complement resistance mechanisms of Klebsiella pneumoniae (2016) Immunobiology, 221, pp. 1102-1109
Drulis-Kawa, Z., Majkowska-Skrobek, G., Maciejewska, B., Bacteriophages and phagederived proteins - Application approaches (2015) Curr. Med. Chem, 22, pp. 1757-1773
Dutton, G.G.S., Choy, Y.M., Capsular polysaccharide from Klebsiella type 21 (1972) Carbohydr. Res., 21, pp. 169-172
Dutton, G.G.S., Parolis, H., Joseleau, J.-P., Marais, M.-F., The use of bacteriophage depolymerization in the structural investigation of the capsular polysaccharide from Klebsiella serotype K3 (1986) Carbohydr. Res., 149, pp. 411-423
Hsieh, P.F., Lin, H.H., Lin, T.L., Chen, Y.Y., Wang, J.T., Two T7-like bacteriophages, K5-2 and K5-4, each encodes two capsule depolymerases: Isolation and functional characterization (2017) Sci. Rep, 7, pp. 1-13
Insua, J.L., Llobet, E., Moranta, D., Pérez-Gutiérrez, C., Tomás, A., Garmendia, J., Modeling Klebsiella pneumoniae pathogenesis by infection of the wax moth Galleria mellonella (2013) Infect. Immun, 81, pp. 3552-3565
Kanamaru, S., Leiman, P.G., Kostyuchenko, V.A., Chipman, P.R., Mesyanzhinov, V.V., Arisaka, F., Structure of the cell-puncturing device of bacteriophage T4 (2002) Nature, 415, pp. 553-557
Kassa, T., Chhibber, S., Thermal treatment of the bacteriophage lysate of Klebsiella pneumoniae B5055 as a step for the purification of capsular depolymerase enzyme (2012) J. Virol. Methods, 179, pp. 135-141
Ksik-Szeloch, A., Drulis-Kawa, Z., Weber-Dabrowska, B., Kassner, J., Majkowska-Skrobek, G., Augustyniak, D., Characterising the biology of novel lytic bacteriophages infecting multidrug resistant Klebsiella pneumoniae (2013) Virol. J, 10, pp. 1-12
Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
Latka, A., Maciejewska, B., Majkowska-Skrobek, G., Briers, Y., Drulis-Kawa, Z., Bacteriophage-encoded virion-associated enzymes to overcome the carbohydrate barriers during the infection process (2017) Appl. Microbiol. Biotechnol., 101, pp. 3103-3119
Lawlor, M.S., Hsu, J., Rick, P.D., Miller, V.L., Identification of Klebsiella pneumoniae virulence determinants using an intranasal infection model (2005) Mol. Microbiol., 58, pp. 1054-1073
Leiman, P.G., Molineux, I.J., Evolution of a new enzyme activity from the same motif fold (2008) Mol. Microbiol., 69, pp. 287-290
Li, X.Y., Lin, Z.Y., Zhu, P.P., Jin, Y.F., Effect of cyclophosphamide on serum complement in mice (1987) Zhongguo Yao Li Xue Bao, 8, pp. 79-83
Lin, T.L., Hsieh, P.F., Huang, Y.T., Lee, W.C., Tsai, Y.T., Su, P.A., Isolation of a bacteriophage and its depolymerase specific for K1 capsule of Klebsiella pneumoniae: Implication in typing and treatment (2014) J. Infect. Dis., 210, pp. 1734-1744
Maciejewska, B., Olszak, T., Drulis-Kawa, Z., Applications of bacteriophages versus phage enzymes to combat and cure bacterial infections: An ambitious and also a realistic application? (2018) Appl. Microbiol. Biotechnol., 102, pp. 2563-2581
March, C., Cano, V., Moranta, D., Llobet, E., Pérez-Gutiérrez, C., Tomás, J.M., Role of bacterial surface structures on the interaction of Klebsiella pneumoniae with phagocytes (2013) PLoS One, 8
Martin, R.M., Bachman, M.A., Colonization, infection, and the accessory genome of Klebsiella pneumoniae (2018) Front. Cell. Infect. Microbiol., 8, p. 4
Merino, S., Camprubi, S., Alberti, S., Benedi, V.J., Tomas, J.M., Mechanisms of Klebsiella pneumoniae resistance to complement-mediated killing (1992) Infect. Immun, 60, pp. 2529-2535
Nassif, X., Sansonetti, P.J., Correlation of the virulence of Klebsiella pneumoniae K1 and K2 with the presence of a plasmid encoding aerobactin (1986) Infect. Immun, 54, pp. 603-608
Olszak, T., Shneider, M.M., Latka, A., Maciejewska, B., Browning, C., Sycheva, L.V., The O-specific polysaccharide lyase from the phage LKA1 tailspike reduces Pseudomonas virulence (2017) Sci. Rep, 7, pp. 1-14
Paczosa, M.K., Mecsas, J., Klebsiella pneumoniae: Going on the offense with a strong defense (2016) Microbiol. Mol. Biol. Rev., 80, pp. 629-661
Pan, Y., Lin, T., Chen, C., Tsai, Y., Klebsiella phage FK64-1 encodes multiple depolymerases for multiple host capsular types (2017) J. Virol., 91
Pan, Y.J., Lin, T.L., Chen, Y.H., Hsu, C.R., Hsieh, P.F., Wu, M.C., Capsular types of Klebsiella pneumoniae revisited by wzc sequencing (2013) PLoS One, 8
Podschun, R., Ullmann, U., Klebsiella spp. as nosocomial pathogens: Epidemiology, taxonomy, typing methods, and pathogenicity factors (1998) Clin. Microbiol. Rev., 11, pp. 589-603
Regueiro, V., Campos, M.A., Pons, J., Albertí, S., Bengoechea, J.A., The uptake of a Klebsiella pneumoniae capsule polysaccharide mutant triggers an inflammatory response by human airway epithelial cells (2006) Microbiology, 152, pp. 555-566
Sahly, H., Keisari, Y., Crouch, E., Sharon, N., Ofek, I., Recognition of bacterial surface polysaccharides by lectins of the innate immune system and its contribution to defense against infection: The case of pulmonary pathogens (2008) Infect. Immun, 76, pp. 1322-1332
Shepherd, V.L., Campbell, E.J., Senior, R.M., Stahl, P.D., Characterization of the mannose/fucose receptor on human mononuclear phagocytes (1982) J. Reticuloendothel. Soc, 32, pp. 423-431
Simpson, D.J., Sacher, J.C., Szymanski, C.M., Exploring the interactions between bacteriophage-encoded glycan binding proteins and carbohydrates (2015) Curr. Opin. Struct. Biol., 34, pp. 69-77
Solovieva, E.V., Myakinina, V.P., Kislichkina, A.A., Krasilnikova, V.M., Verevkin, V.V., Mochalov, V.V., Comparative genome analysis of novel Podoviruses lytic for hypermucoviscous Klebsiella pneumoniae of K1. K2, and K57 capsular types (2018) Virus Res., 243, pp. 10-18
Steinbacher, S., Seckler, R., Miller, S., Steipe, B., Huber, R., Reinemer, P., Crystal structure of P22 tailspike protein: Interdigitated subunits in a thermostable trimer (1994) Science, 265, pp. 383-386
Weigele, P.R., Scanlon, E., King, J., Homotrimeric, β-stranded viral adhesins and tail proteins (2003) J. Bacteriol., 185, pp. 4022-4030
Wileman, T.E., Lennartz, M.R., Stahl, P.D., Identification of the macrophage mannose receptor as a 175-kDa membrane protein (1986) Proc. Natl. Acad. Sci. U. S. A., 83, pp. 2501-2505
Wyres, K.L., Wick, R.R., Gorrie, C., Jenney, A., Follador, R., Thomson, N.R., Identification of Klebsiella capsule synthesis loci from whole genome data (2016) Microb. Genomics, 2, pp. 1-15
Yoshida, K., Matsumoto, T., Tateda, K., Uchida, K., Tsujimoto, S., Yamaguchi, K., Role of bacterial capsule in local and systemic inflammatory responses of mice during pulmonary infection with Klebsiella pneumoniae (2000) J. Med. Microbiol., 49, pp. 1003-1010
Phage-Borne Depolymerases Decrease Klebsiella pneumoniae Resistance to Innate Defense Mechanisms
Klebsiella pneumoniae produces capsular polysaccharides that are a crucial virulence factor protecting bacteria against innate response mechanisms of the infected host. Simultaneously, those capsules are targeted by specific bacteriophages equipped with virion-associated depolymerases able to recognize and degrade these polysaccharides. We show that Klebsiella phage KP32 produces two capsule depolymerases, KP32gp37 and KP32gp38, with a high specificity for the capsular serotypes K3 and K21, respectively. Together, they determine the host spectrum of bacteriophage KP32, which is limited to strains with serotype K3 and K21. Both depolymerases form a trimeric β-structure, display moderate thermostability and function optimally under neutral to alkaline conditions. We show that both depolymerases strongly affect the virulence of K. pneumoniae with the corresponding K3 and K21 capsular serotypes. Capsule degradation renders the otherwise serumresistant cells more prone to complement-mediated killing with up to four log reduction in serum upon exposure to KP32gp37. Decapsulated strains are also sensitized for phagocytosis with a twofold increased uptake. In addition, the intracellular survival of phagocytized cells in macrophages was significantly reduced when bacteria were previously exposed to the capsule depolymerases. Finally, depolymerase application considerably increases the lifespan of Galleria mellonella larvae infected with K. pneumoniae in a time- and strain-dependent manner. In sum, capsule depolymerases are promising antivirulence compounds that act by defeating a major resistance mechanism of K. pneumoniae against the innate immunity. © 2018 Departamento de Enfermagem/Universidade Federal de Sao Paulo. All rights reserved.
Klebsiella pneumoniae produces capsular polysaccharides that are a crucial virulence factor protecting bacteria against innate response mechanisms of the infected host. Simultaneously, those capsules are targeted by specific bacteriophages equipped with virion-associated depolymerases able to recognize and degrade these polysaccharides. We show that Klebsiella phage KP32 produces two capsule depolymerases, KP32gp37 and KP32gp38, with a high specificity for the capsular serotypes K3 and K21, respectively. Together, they determine the host spectrum of bacteriophage KP32, which is limited to strains with serotype K3 and K21. Both depolymerases form a trimeric β-structure, display moderate thermostability and function optimally under neutral to alkaline conditions. We show that both depolymerases strongly affect the virulence of K. pneumoniae with the corresponding K3 and K21 capsular serotypes. Capsule degradation renders the otherwise serumresistant cells more prone to complement-mediated killing with up to four log reduction in serum upon exposure to KP32gp37. Decapsulated strains are also sensitized for phagocytosis with a twofold increased uptake. In addition, the intracellular survival of phagocytized cells in macrophages was significantly reduced when bacteria were previously exposed to the capsule depolymerases. Finally, depolymerase application considerably increases the lifespan of Galleria mellonella larvae infected with K. pneumoniae in a time- and strain-dependent manner. In sum, capsule depolymerases are promising antivirulence compounds that act by defeating a major resistance mechanism of K. pneumoniae against the innate immunity. © 2018 Departamento de Enfermagem/Universidade Federal de Sao Paulo. All rights reserved.
Phage-Borne Depolymerases Decrease Klebsiella pneumoniae Resistance to Innate Defense Mechanisms
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Phage-Borne Depolymerases Decrease Klebsiella pneumoniae Resistance to Innate Defense Mechanisms
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Viruses-Basel (ISSN: 1999-4915), 2016 Dec 1; 8(12): N/D-N/D.
Impact Factor: 3.465
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Molinaro A, Holst O, Lorenzo FD, Callaghan M, Nurisso A, D'Errico G, Zamyatina A, Peri F, Berisio R, Jerala R, Jiménez-Barbero J, Silipo A, Martín-Santamarí S
* Chemistry of lipid a: At the heart of innate immunity (1277 views) (PDF 305 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2015 Jan 7; 21(2): 500-519.
Impact Factor: 5.771
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Speciale I, Paciello I, Fazio LL, Sturiale L, Palmigiano A, Lanzetta R, Parrilli M, Garozzo D, Lemaitre B, Bernardini ML, Molinaro A, De Castro C
* Determination of the structure of the O-antigen and the lipid A from the entomopathogenic bacterium Pseudomonas entomophila lipopolysaccharide along with its immunological properties (387 views)
Carbohyd Res (ISSN: 0008-6215, 0008-6215linking), 2015; 412: 20-27.
Impact Factor: 1.817
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Di Lorenzo F, Silipo A, Bianconi I, Lore' NI, Scamporrino A, Sturiale L, Garozzo D, Lanzetta R, Parrilli M, Bragonzi A, Molinaro A
* Persistent cystic fibrosis isolate Pseudomonas aeruginosa strain RP73 exhibits an under-acylated LPS structure responsible of its low inflammatory activity (364 views)
Mol Immunol (ISSN: 0161-5890), 2015; 63(2): 166-175.
Impact Factor: 3.375
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Galdiero S, Falanga A, Vitiello M, Grieco P, Caraglia M, Morelli G, Galdiero M
* Exploitation of viral properties for intracellular delivery (508 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617linking), 2014 Jul; 20(7): 468-478.
Impact Factor: 1.546
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Causa F, Della Moglie R, Iaccino E, Mimmi S, Marasco D, Scognamiglio PL, Battista E, Palmieri C, Cosenza C, Sanguigno L, Quinto I, Scala G, Netti PA
* Evolutionary screening and adsorption behavior of engineered M13 bacteriophage and derived dodecapeptide for selective decoration of gold interfaces (412 views)
J Colloid Interface Sci (ISSN: 0021-9797, 1095-7103electronic, 0021-9797linking), 2013 Jan 1; 389(1): 220-229.
Impact Factor: 1.646
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Berisio R
* Learning from pathogens: Exploiting host-pathogen liaison for therapeutic development (523 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2012 Dec; 13(8): 697-698.
Impact Factor: 2.326
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Berisio R
* Editorial: cell processes in bacterial diseases (409 views)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2012 Oct; 19(10): 1011-1012.
Impact Factor: 1.994
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De Simone G
* Editorial: Zinc Metallo-Enzymes As Target For Drug Design (423 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2012 Feb; 19(6): 820-1012.
Impact Factor: 4.07
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Cho WG, Albuquerque RJ, Kleinman ME, Tarallo V, Greco A, Nozaki M, Green MG, Baffi JZ, Ambati BK, De Falco M, Alexander JS, Brunetti A, De Falco S, Ambati J
* Small interfering RNA-induced TLR3 activation inhibits blood and lymphatic vessel growth (403 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2009 Apr 28; 106(17): 7137-7142.
Impact Factor: 9.432
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* Defense Against Pathogens: Structural Insights into the Mechanism of Chitin Induced Activation of Innate Immunity (267 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2017 Nov 24; 24(36): 3980-3986.
Impact Factor: 3.469
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Majkowska-skrobek G, Latka A, Berisio R, Maciejewska B, Squeglia F, RomanoM, Lavigne R, Struve C, Drulis-kawa Z
* Capsule-Targeting Depolymerase, Derived from Klebsiella KP36 Phage, as a Tool for the Development of Anti-Virulent Strategy (355 views)
Viruses-Basel (ISSN: 1999-4915), 2016 Dec 1; 8(12): N/D-N/D.
Impact Factor: 3.465
View Export to BibTeX Export to EndNote
Molinaro A, Holst O, Lorenzo FD, Callaghan M, Nurisso A, D'Errico G, Zamyatina A, Peri F, Berisio R, Jerala R, Jiménez-Barbero J, Silipo A, Martín-Santamarí S
* Chemistry of lipid a: At the heart of innate immunity (1277 views) (PDF 305 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2015 Jan 7; 21(2): 500-519.
Impact Factor: 5.771
View Export to BibTeX Export to EndNote
Speciale I, Paciello I, Fazio LL, Sturiale L, Palmigiano A, Lanzetta R, Parrilli M, Garozzo D, Lemaitre B, Bernardini ML, Molinaro A, De Castro C
* Determination of the structure of the O-antigen and the lipid A from the entomopathogenic bacterium Pseudomonas entomophila lipopolysaccharide along with its immunological properties (387 views)
Carbohyd Res (ISSN: 0008-6215, 0008-6215linking), 2015; 412: 20-27.
Impact Factor: 1.817
View Export to BibTeX Export to EndNote
Di Lorenzo F, Silipo A, Bianconi I, Lore' NI, Scamporrino A, Sturiale L, Garozzo D, Lanzetta R, Parrilli M, Bragonzi A, Molinaro A
* Persistent cystic fibrosis isolate Pseudomonas aeruginosa strain RP73 exhibits an under-acylated LPS structure responsible of its low inflammatory activity (364 views)
Mol Immunol (ISSN: 0161-5890), 2015; 63(2): 166-175.
Impact Factor: 3.375
View Export to BibTeX Export to EndNote
Galdiero S, Falanga A, Vitiello M, Grieco P, Caraglia M, Morelli G, Galdiero M
* Exploitation of viral properties for intracellular delivery (508 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617linking), 2014 Jul; 20(7): 468-478.
Impact Factor: 1.546
View Export to BibTeX Export to EndNote
Causa F, Della Moglie R, Iaccino E, Mimmi S, Marasco D, Scognamiglio PL, Battista E, Palmieri C, Cosenza C, Sanguigno L, Quinto I, Scala G, Netti PA
* Evolutionary screening and adsorption behavior of engineered M13 bacteriophage and derived dodecapeptide for selective decoration of gold interfaces (412 views)
J Colloid Interface Sci (ISSN: 0021-9797, 1095-7103electronic, 0021-9797linking), 2013 Jan 1; 389(1): 220-229.
Impact Factor: 1.646
View Export to BibTeX Export to EndNote
Berisio R
* Learning from pathogens: Exploiting host-pathogen liaison for therapeutic development (523 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2012 Dec; 13(8): 697-698.
Impact Factor: 2.326
View Export to BibTeX Export to EndNote
Berisio R
* Editorial: cell processes in bacterial diseases (409 views)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2012 Oct; 19(10): 1011-1012.
Impact Factor: 1.994
View Export to BibTeX Export to EndNote
De Simone G
* Editorial: Zinc Metallo-Enzymes As Target For Drug Design (423 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2012 Feb; 19(6): 820-1012.
Impact Factor: 4.07
View Export to BibTeX Export to EndNote
Cho WG, Albuquerque RJ, Kleinman ME, Tarallo V, Greco A, Nozaki M, Green MG, Baffi JZ, Ambati BK, De Falco M, Alexander JS, Brunetti A, De Falco S, Ambati J
* Small interfering RNA-induced TLR3 activation inhibits blood and lymphatic vessel growth (403 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2009 Apr 28; 106(17): 7137-7142.
Impact Factor: 9.432
View Export to BibTeX Export to EndNote
11 Records (11 excluding Abstracts).
Total impact factor: 38.911 (38.911 excluding Abstracts).
Total 5 year impact factor: 41.559 (41.559 excluding Abstracts).
Total impact factor: 38.911 (38.911 excluding Abstracts).
Total 5 year impact factor: 41.559 (41.559 excluding Abstracts).
374 views. Last view on Monday 27 March 2023, 18:04:03
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