A carcinoembryonic antigen-related cell adhesion molecule 1 homologue plays a pivotal role in nontypeable Haemophilus influenzae colonization of the chinchilla nasopharynx via the outer membrane protein P5-homologous adhesin

Infect Immun. 2008 Jan;76(1):48-55. doi: 10.1128/IAI.00980-07. Epub 2007 Oct 15.

Abstract

In vitro studies suggest an important role for CEACAM1 (carcinoembryonic antigen-related cell adhesion molecule 1) in infection by multiple gram-negative bacteria. However, in vivo evidence supporting this role is lacking, largely because the bacterial adhesins involved in this host-microbe association do not bind to murine-derived CEACAM1. One of several adhesins expressed by nontypeable Haemophilus influenzae (NTHI), the outer membrane protein P5-homologous adhesin (or P5), is essential for colonization of the chinchilla nasopharynx and infection of the middle ear. Here we reveal that NTHI P5 binds to the chinchilla homologue of CEACAM1 and that rabbit anti-human carcinoembryonic antigen blocks NTHI colonization of the chinchilla nasopharynx, providing the first demonstration of a role for CEACAM receptor binding by any bacterial pathogen in vivo.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antigens, CD / chemistry
  • Antigens, CD / metabolism*
  • Bacterial Outer Membrane Proteins / metabolism*
  • Carrier State
  • Cell Adhesion Molecules / chemistry
  • Cell Adhesion Molecules / metabolism*
  • Chinchilla / microbiology*
  • Gene Expression Regulation
  • Haemophilus influenzae / physiology*
  • HeLa Cells
  • Humans
  • Nasopharynx / microbiology*

Substances

  • Antigens, CD
  • Bacterial Outer Membrane Proteins
  • CD66 antigens
  • Cell Adhesion Molecules
  • OMPA outer membrane proteins