Affordable Access

Publisher Website

Mapping the Laminin Receptor Binding Domains of Neisseria meningitidis PorA and Haemophilus influenzae OmpP2

Authors
Journal
PLoS ONE
1932-6203
Publisher
Public Library of Science
Publication Date
Volume
7
Issue
9
Identifiers
DOI: 10.1371/journal.pone.0046233
Keywords
  • Research Article
  • Biology
  • Microbiology
  • Bacterial Pathogens
  • Gram Negative
  • Host-Pathogen Interaction
  • Medical Microbiology
  • Microbial Pathogens
  • Pathogenesis
  • Medicine
  • Infectious Diseases
  • Bacterial Diseases
  • Haemophilus Influenzae
  • Meningitis
  • Meningoccal Septicemia
  • Meningococcal Disease
  • Meningococcal Infections
  • Infectious Diseases Of The Nervous System
Disciplines
  • Biology

Abstract

Neisseria meningitidis, Haemophilus influenzae and Streptococcus pneumoniae are major bacterial agents of meningitis. They each bind the 37/67-kDa laminin receptor (LamR) via the surface protein adhesins: meningococcal PilQ and PorA, H. influenzae OmpP2 and pneumococcal CbpA. We have previously reported that a surface-exposed loop of the R2 domain of CbpA mediates LamR-binding. Here we have identified the LamR-binding regions of PorA and OmpP2. Using truncated recombinant proteins we show that binding is dependent on amino acids 171–240 and 91–99 of PorA and OmpP2, respectively, which are predicted to localize to the fourth and second surface-exposed loops, respectively, of these proteins. Synthetic peptides corresponding to the loops bound LamR and could block LamR-binding to bacterial ligands in a dose dependant manner. Meningococci expressing PorA lacking the apex of loop 4 and H. influenzae expressing OmpP2 lacking the apex of loop 2 showed significantly reduced LamR binding. Since both loops are hyper-variable, our data may suggest a molecular basis for the range of LamR-binding capabilities previously reported among different meningococcal and H. influenzae strains.

There are no comments yet on this publication. Be the first to share your thoughts.