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The Opacity Family [Function: Adhesion] Seed alignment | Full alignment in OMPdb

Members of this family are homologs to the surface protein A (NspA) from Neisseria meningitidis, which is a promising vaccine candidate. NspA is a highly conserved membrane protein that elicits protective antibody responses in mice against Neisseria meningitidis infection. NspA forms an 8-stranded antiparallel ß-barrel, whereas 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. Loops 2 and 3, are more important regarding antibody binding.


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Literature references

Conformational epitopes recognized by protective anti-neisserial surface protein A antibodies
Infect Immun. 2003 Dec;71(12):6844-9. doi: 10.1128/iai.71.12.6844-6849.2003.
PMID: 14638771

Highly conserved Neisseria meningitidis surface protein confers protection against experimental infection
J Exp Med. 1997 Apr 7;185(7):1173-83. doi: 10.1084/jem.185.7.1173.
PMID: 9104804

The role of neisserial Opa proteins in interactions with host cells
Trends Microbiol. 1998 Dec;6(12):489-95. doi: 10.1016/s0966-842x(98)01365-1.
PMID: 10036728

Crystal structure of Neisserial surface protein A (NspA), a conserved outer membrane protein with vaccine potential
J Biol Chem. 2003 Jul 4;278(27):24825-30. doi: 10.1074/jbc.M302803200. Epub 2003 Apr 26.
PMID: 12716881

Proteins in this family with 3D-structure

Q9RP17

Q04884


Elixir UTH dib compgen