Dimerisation and structural integrity of Heparin Binding Hemagglutinin A from Mycobacterium tuberculosis: Implications for bacterial agglutination(494 views) Esposito C, Carullo C, Pedone E, Graziano G, Del Vecchio P, Berisio R
Febs Lett (ISSN: 0014-5793, 0014-5793print, 0014-5793linking), 2010 Mar 19; 584(6): 1091-1096.
Istitute of Biostructures and Bioimaging, C.N.R., I-80134 - Naples, Italy
Department of Chemistry Paolo Corradini, University of Naples Federico II, Complesso Universitario Monte S. Angelo, I-80126, Naples, Italy
Department of Biological and Environmental Sciences, University of Sannio, I-82100 Benevento, Italy
References: Menozzi, F.D., Bischoff, R., Fort, E., Brennan, M.J., Locht, C., Molecular characterization of the mycobacterial heparin-binding hemagglutinin, a mycobacterial adhesin (1998) Proc. Natl. Acad. Sci. USA, 95, pp. 12625-1263
Pethe, K., Alonso, S., Biet, F., Delogu, G., Brennan, M.J., Locht, C., Menozzi, F.D., The heparin-binding haemagglutinin of M. tuberculosis is required for extrapulmonary dissemination (2001) Nature, 412, pp. 190-194
Pethe, K., Aumercier, M., Fort, E., Gatot, C., Locht, C., Menozzi, F.D., Characterization of the heparin-binding site of the mycobacterial heparin-binding hemagglutinin adhesin (2000) J. Biol. Chem., 275, pp. 14273-14280
Heise, T., Dersch, P., Identification of a domain in Yersinia virulence factor YadA that is crucial for extracellular matrix-specific cell adhesion and uptake (2006) Proc. Natl. Acad. Sci. USA, 103, pp. 3375-3380
Verbelen, C., Raze, D., Dewitte, F., Locht, C., Dufrene, Y.F., Single-molecule force spectroscopy of mycobacterial adhesin-adhesin interactions (2007) J. Bacteriol., 189, pp. 8801-8806
Esposito, C., Pethoukov, M.V., Svergun, D.I., Ruggiero, A., Pedone, C., Pedone, E., Berisio, R., Evidence for an elongated dimeric structure of heparin-binding hemagglutinin from Mycobacterium tuberculosis (2008) J. Bacteriol., 190, pp. 4749-4753
Barone, G., Del Vecchio, P., Fessas, D., Giancola, C., Graziano, G., (1992) J. Therm. Anal., 38, p. 2779
Privalov, P.L., Stability of proteins: small globular proteins (1979) Adv. Protein Chem., 33, pp. 167-241
Zhou, Y., Hall, C.K., Karplus, M., The calorimetric criterion for a two-state process revisited (1999) Protein Sci., 8, pp. 1064-1074
Kleywegt, G.J., Jones, T.A., Model building and refinement practice (1997) Methods Enzymol., 277, pp. 208-230
Van Der Spoel, D., Lindahl, E., Hess, B., Groenhof, G., Mark, A.E., Berendsen, H.J., GROMACS: fast, flexible, and free (2005) J. Comput. Chem., 26, pp. 1701-1718
Walshaw, J., Woolfson, D.N., Socket: a program for identifying and analysing coiled-coil motifs within protein structures (2001) J. Mol. Biol., 307, pp. 1427-1450
Steinmetz, M.O., Molecular basis of coiled-coil formation (2007) Proc. Natl. Acad. Sci. USA, 104, pp. 7062-7067
Wolf, E., Kim, P.S., Berger, B., MultiCoil: a program for predicting two- and three-stranded coiled coils (1997) Protein Sci., 6, pp. 1179-1189
Hofmann, K., Stoffel, W., TMbase - a database of membrane spanning proteins segments (1993) Biol. Chem. Hoppe-Seyler, 374, p. 166
Jones, D.T., Taylor, W.R., Thornton, J.M., A model recognition approach to the prediction of all-helical membrane protein structure and topology (1994) Biochemistry, 33, pp. 3038-3049
Kall, L., Krogh, A., Sonnhammer, E.L., Advantages of combined transmembrane topology and signal peptide prediction-the Phobius web server (2007) Nucleic Acids Res., 35, pp. W429-W432
Hoffmann, C., Leis, A., Niederweis, M., Plitzko, J.M., Engelhardt, H., Disclosure of the mycobacterial outer membrane: cryo-electron tomography and vitreous sections reveal the lipid bilayer structure (2008) Proc. Natl. Acad. Sci. USA, 105, pp. 3963-3967
Niederweis, M., Danilchanka, O., Huff, J., Hoffmann, C., Engelhardt, H., (2010), Mycobacterial outer membranes: in search of proteins. Trends Microbiol., in pressNewman, J.R., Wolf, E., Kim, P.S., A computationally directed screen identifying interacting coiled coils from Saccharomyces cerevisiae (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 13203-13208
Hurme, R., Berndt, K.D., Normark, S.J., Rhen, M., A proteinaceous gene regulatory thermometer in Salmonella (1997) Cell, 90, pp. 55-64
McFarlane, A.A., Orriss, G.L., Stetefeld, J., The use of coiled-coil proteins in drug delivery systems (2009) Eur. J. Pharmacol., 625, pp. 101-107
Meier, M., Burkhard, P., Statistical analysis of intrahelical ionic interactions in alpha-helices and coiled coils (2006) J. Struct. Biol., 155, pp. 116-129
Lee, D.L., Lavigne, P., Hodges, R.S., Are trigger sequences essential in the folding of two-stranded alpha-helical coiled-coils? (2001) J. Mol. Biol., 306, pp. 539-553
Tan, K., Heparin-induced cis- and trans-dimerization modes of the thrombospondin-1 N-terminal domain (2008) J. Biol. Chem., 283, pp. 3932-3941
Goodger, S.J., Robinson, C.J., Murphy, K.J., Gasiunas, N., Harmer, N.J., Blundell, T.L., Pye, D.A., Gallagher, J.T., Evidence that heparin saccharides promote FGF2 mitogenesis through two distinct mechanisms (2008) J. Biol. Chem., 283, pp. 13001-13008
Soba, P., Homo- and heterodimerization of APP family members promotes intercellular adhesion (2005) EMBO J., 24, pp. 3624-3634
Menozzi, F. D., Bischoff, R., Fort, E., Brennan, M. J., Locht, C., Molecular characterization of the mycobacterial heparin-binding hemagglutinin, a mycobacterial adhesin (1998) Proc. Natl. Acad. Sci. USA, 95, pp. 12625-1263
Privalov, P. L., Stability of proteins: small globular proteins (1979) Adv. Protein Chem., 33, pp. 167-241
Zhou, Y., Hall, C. K., Karplus, M., The calorimetric criterion for a two-state process revisited (1999) Protein Sci., 8, pp. 1064-1074
Kleywegt, G. J., Jones, T. A., Model building and refinement practice (1997) Methods Enzymol., 277, pp. 208-230
Steinmetz, M. O., Molecular basis of coiled-coil formation (2007) Proc. Natl. Acad. Sci. USA, 104, pp. 7062-7067
Wolf, E., Kim, P. S., Berger, B., MultiCoil: a program for predicting two- and three-stranded coiled coils (1997) Protein Sci., 6, pp. 1179-1189
Jones, D. T., Taylor, W. R., Thornton, J. M., A model recognition approach to the prediction of all-helical membrane protein structure and topology (1994) Biochemistry, 33, pp. 3038-3049
McFarlane, A. A., Orriss, G. L., Stetefeld, J., The use of coiled-coil proteins in drug delivery systems (2009) Eur. J. Pharmacol., 625, pp. 101-107
Lee, D. L., Lavigne, P., Hodges, R. S., Are trigger sequences essential in the folding of two-stranded alpha-helical coiled-coils? (2001) J. Mol. Biol., 306, pp. 539-553
Goodger, S. J., Robinson, C. J., Murphy, K. J., Gasiunas, N., Harmer, N. J., Blundell, T. L., Pye, D. A., Gallagher, J. T., Evidence that heparin saccharides promote FGF2 mitogenesis through two distinct mechanisms (2008) J. Biol. Chem., 283, pp. 13001-13008
Dimerisation and structural integrity of Heparin Binding Hemagglutinin A from Mycobacterium tuberculosis: Implications for bacterial agglutination