Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M302803200 on April 26, 2003

J. Biol. Chem., Vol. 278, Issue 27, 24825-24830, July 4, 2003
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
278/27/24825    most recent
M302803200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Vandeputte-Rutten, L.
Right arrow Articles by Gros, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vandeputte-Rutten, L.
Right arrow Articles by Gros, P.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Crystal Structure of Neisserial Surface Protein A (NspA), a Conserved Outer Membrane Protein with Vaccine Potential*

Lucy Vandeputte-Rutten {ddagger}, Martine P. Bos § ¶, Jan Tommassen § and Piet Gros {ddagger} ||

From the {ddagger}Department of Crystal and Structural Chemistry, Bijvoet Center for Biomolecular Research and the §Department of Molecular Microbiology, Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands

The neisserial surface protein A (NspA) from Neisseria meningitidis is a promising vaccine candidate because it is highly conserved among meningococcal strains and induces bactericidal antibodies. NspA is a homolog of the Opa proteins, which mediate adhesion to host cells. Here, we present the crystal structure of NspA, determined to 2.55-Å resolution. NspA forms an eight-stranded antiparallel {beta}-barrel. The four loops at the extracellular side of the NspA molecule form a long cleft, which contains mainly hydrophobic residues and harbors a detergent molecule, suggesting that the protein might function in the binding of hydrophobic ligands, such as lipids. In addition, the structure provides a starting point for structure-based vaccine design.


Received for publication, March 19, 2003 , and in revised form, April 24, 2003.

The atomic coordinates and structure factors (code 1P4T) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

* This work was supported by the council for Chemical Sciences of the Netherlands Organization for Scientific Research (NWO-CW). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by the European Community project MenB vaccine QLRT-1999-CT-00359.

|| To whom correspondence should be addressed. Tel.: 31-30-2533502; Fax: 31-30-2533940; E-mail: p.gros{at}chem.uu.nl.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Bacteriol.Home page
Y. Kumagai, H. Huang, and Y. Rikihisa
Expression and Porin Activity of P28 and OMP-1F during Intracellular Ehrlichia chaffeensis Development
J. Bacteriol., May 15, 2008; 190(10): 3597 - 3605.
[Abstract] [Full Text] [PDF]


Home page
CVIHome page
G. Norheim, A. Aseffa, M. A. Yassin, G. Mengistu, A. Kassu, D. Fikremariam, W. Tamire, Y. Merid, E. A. Hoiby, D. A. Caugant, et al.
Specificity of Subcapsular Antibody Responses in Ethiopian Patients following Disease Caused by Serogroup A Meningococci
Clin. Vaccine Immunol., May 1, 2008; 15(5): 863 - 871.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
V. E. Weynants, C. M. Feron, K. K. Goraj, M. P. Bos, P. A. Denoel, V. G. Verlant, J. Tommassen, I. R. A. Peak, R. C. Judd, M. P. Jennings, et al.
Additive and Synergistic Bactericidal Activity of Antibodies Directed against Minor Outer Membrane Proteins of Neisseria meningitidis
Infect. Immun., November 1, 2007; 75(11): 5434 - 5442.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
M. J. Brooks, C. A. Laurence, E. J. Hansen, and S. D. Gray-Owen
Characterization of the Moraxella catarrhalis Opa-Like Protein, OlpA, Reveals a Phylogenetically Conserved Family of Outer Membrane Proteins
J. Bacteriol., January 1, 2007; 189(1): 76 - 82.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
L. Rutten, J. Geurtsen, W. Lambert, J. J. M. Smolenaers, A. M. Bonvin, A. de Haan, P. van der Ley, M. R. Egmond, P. Gros, and J. Tommassen
Crystal structure and catalytic mechanism of the LPS 3-O-deacylase PagL from Pseudomonas aeruginosa
PNAS, May 2, 2006; 103(18): 7071 - 7076.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
F. Cantini, S. Savino, M. Scarselli, V. Masignani, M. Pizza, G. Romagnoli, E. Swennen, D. Veggi, L. Banci, and R. Rappuoli
Solution Structure of the Immunodominant Domain of Protective Antigen GNA1870 of Neisseria meningitidis
J. Biol. Chem., March 17, 2006; 281(11): 7220 - 7227.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
H. Hong, D. R. Patel, L. K. Tamm, and B. van den Berg
The Outer Membrane Protein OmpW Forms an Eight-stranded beta-Barrel with a Hydrophobic Channel
J. Biol. Chem., March 17, 2006; 281(11): 7568 - 7577.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
J. P. Hays, S. van Selm, T. Hoogenboezem, S. Estevao, K. Eadie, P. van Veelen, J. Tommassen, A. van Belkum, and P. W. M. Hermans
Identification and Characterization of a Novel Outer Membrane Protein (OMP J) of Moraxella catarrhalis That Exists in Two Major Forms
J. Bacteriol., December 1, 2005; 187(23): 7977 - 7984.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. Moore, S. E. S. Bailey, Z. Benmechernene, C. Tzitzilonis, N. J. E. Griffiths, M. Virji, and J. P. Derrick
Recognition of Saccharides by the OpcA, OpaD, and OpaB Outer Membrane Proteins from Neisseria meningitidis
J. Biol. Chem., September 9, 2005; 280(36): 31489 - 31497.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
M. M. Giuliani, L. Santini, B. Brunelli, A. Biolchi, B. Arico, F. Di Marcello, E. Cartocci, M. Comanducci, V. Masignani, L. Lozzi, et al.
The Region Comprising Amino Acids 100 to 255 of Neisseria meningitidis Lipoprotein GNA 1870 Elicits Bactericidal Antibodies
Infect. Immun., February 1, 2005; 73(2): 1151 - 1160.
[Abstract] [Full Text] [PDF]


Home page
Microbiol. Mol. Biol. Rev.Home page
H. Nikaido
Molecular Basis of Bacterial Outer Membrane Permeability Revisited
Microbiol. Mol. Biol. Rev., December 1, 2003; 67(4): 593 - 656.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
V. C. Hou, G. R. Moe, Z. Raad, T. Wuorimaa, and D. M. Granoff
Conformational Epitopes Recognized by Protective Anti-Neisserial Surface Protein A Antibodies
Infect. Immun., December 1, 2003; 71(12): 6844 - 6849.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement