Structural requirements for proinflammatory activity of porin P2 loop 7 from Haemophilus influenzae(514 views) Galdiero S, Vitiello M, Amodeo P, D'Isanto M, Cantisani M, Pedone C, Galdiero M
Department of Experimental Medicine, II University of Naples, Via De Crecchio 7, 80138 Naples, Italy
Department of Biological Sciences, University of Naples Federico II, Istituto di Biostrutture e Bioimmagini-CNR, Via Mezzocannone 16, 80134 Naples, Italy
Istituto di Chimica Biomolecolare-CNR, Sede di Pozzuoli, Comprensorio Olivetti, Via Campi Flegrei 34, 80078 Pozzuoli, Naples, Italy
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Yi, K., Murphy, T. F., Importance of an immunodominant surface-exposed loop on outer membrane protein P2 of nontypeable Haemophilus influenzae (1997) Infect. Immun., 65, pp. 150-155
Sikkema, D. J., Murphy, T. F., Molecular analysis of the P2 porin protein of nontypeable Haemophilus influenzae (1992) Infect. Immun., 60, pp. 5204-5211
Saint, N., Lou, K. L., Widmer, C., Luckey, M., Schirmer, T., Rosenbusch, J. P., Structural and functional characterization of OmpF porin mutants selected for larger pore size. II. Functional characterization (1996) J. Biol. Chem., 271, pp. 20676-20680
Dinarello, C. A., The proinflammatory cytokines interleukin-1 and tumor necrosis factor and treatment of the septic shock syndrome (1991) J. Infect. Dis., 163, pp. 1177-1184
Van Amersfoort, E. S., Van Berkel, T. J., Kuiper, J., Receptors, mediators, and mechanisms involved in bacterial sepsis and septic shock (2003) Clin. Microbiol. Rev., 16, pp. 379-414
Coulton, J. W., Wan, I. F., The outer membrane of Haemophilus influenzae type b: Cell envelope associations of major proteins (1983) Can. J. Microbiol., 29, pp. 280-287
Lowry, O. H., Rosebrough, N. J., Farr, A. L., Randall, R. J., Protein measurement with the Polin phenol reagent (1951) J. Biol. Chem., 193, pp. 265-275
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Tsai, C. M., Frasch, C. E., A sensitive silver stain for detecting lipopolysaccharides in polyacrylamide gels (1982) Anal. Biochem., 119, pp. 115-119
Yin, E. T., Galanos, C., Kinsky, S., Bradshaw, R. A., Wessler, S., Luderity, O., Sarmiento, M. F., Picogram-sensitive assay for endotoxin: Gelation of Limulus polyphemus blood cell lysate induced by purified lipopolysaccharides and lipid a from Gram-negative bacteria (1972) Biochim. Blophys. Acta, 261, pp. 284-289
Simmerling, C. L., Darden, T. A., Merz, K. M., Stanton, R. V., Cheng, A. L., Vincent, J. J., Crowley, M., Duan, Y., (1999) AMBER 6, , University of California, San Francisco, CA
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Jorgensen, W. L., Chandrasekhar, J., Madura, J., Klein, M. L., Comparison of simple potential functions for simulating liquid water (1983) J. Chem. Phys., 79, pp. 926-935
Vitale, R. M., Zaccaro, L., Di Blasio, B., Fattorusso, R., Isernia, C., Amodeo, P., Pedone, C., Saviano, M., Conformational features of human melanin-concentrating hormone: An NMR and computational analysis (2003) ChemBioChem, 4, pp. 73-81
Berman, H. M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T. N., Weissig, H., Shindyalov, I. N., Bourne, P. E., The protein data bank (2000) Nucleic Acids Res., 28, pp. 235-242
Hutchinson, E. G., Thornton, J. M., A revised set of potentials for beta-turn formation in proteins (1994) Protein Sci., 3, pp. 2207-2216
Li, S., Kelly, S. J., Lamani, E., Ferraroni, M., Jedrzejas, M. J., Structural basis of hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase (2000) EMBO J., 19, pp. 1228-1240
Singh, S. K., Matsuno, K., LaPorte, D. C., Banaszak, L. J., Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1. 55. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase (2001) J. Biol. Chem., 276, pp. 26154-26163
Muller, D. J., Engel, A., Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy (1999) J. Mol. Biol., 285, pp. 1347-1351
Structural requirements for proinflammatory activity of porin P2 loop 7 from Haemophilus influenzae
Haemophilus influenzae type b (Hib) is one of the leading causes of invasive bacterial infection in young children, characterized by inflammation mainly mediated by cytokines and chemokines. One of the most abundant components of the Hib outer membrane is the P2 porin, which has been shown to induce the release of several inflammatory cytokines. Synthetic peptides corresponding to loops L5, L6, and L7 activate JNK and p38 mitogen-activated protein kinase (MAPK) pathways, L7 being the most active peptide. Therefore, sequence-activity relationships and key residues were identified by elongating sequence to different extents, designing cyclic peptides, and performing an alanine scan of L7. The ability of mutant peptides to induce activation of signal transduction pathways and release of TNF-alpha and IL-6 has been determined, and, in conjunction with CD spectra, bioinformatics analysis, and molecular dynamics data, showed that 6 out of 8 amino acids contribute significantly to the overall activity. Molecular dynamics showed that L7 modifications increased loop rigidity and helicity after Gly6 mutation, thus, providing a possible structural explanation for observed loss of bioactivity. This work provides insights into essential molecular details of P2 that may impact on the pathogenesis of Hib infections where interruption of the signaling cascade could represent an attractive therapeutic strategy.
Structural requirements for proinflammatory activity of porin P2 loop 7 from Haemophilus influenzae
Kállay C, Dávid A, Timári S, Nagy EM, Sanna D, Garribba E, Micera G, De Bona P, Pappalardo G, Rizzarelli E, Sóvágó I * Copper(II) complexes of rat amylin fragments(357 views) Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2011 Oct 14; 40(38): 9711-9721. Impact Factor:3.838 ViewExport to BibTeXExport to EndNote