PMID: 8106776Feb 1, 1994Paper

High-molecular-weight surface-exposed proteins of Haemophilus influenzae mediate binding to macrophages

The Journal of Infectious Diseases
G J NoelD M Mosser

Abstract

The molecular basis for direct bacteria-macrophage interactions that distinguishes nontypeable (NT) Haemophilus influenzae from type b organisms is not known. Because of similarities between filamentous hemagglutinin (FHA) adhesin of Bordetella pertussis and high-molecular-weight (HMW) proteins commonly expressed by NT H. influenzae, the role that HMW proteins play in determining NT H. influenzae-macrophage interactions was assessed. In tests with genetically engineered organisms, HMW protein-expressing bacteria bound significantly better than isogenic HMW protein-deficient bacteria to macrophages. HMW protein-dependent binding to macrophages is trypsin-sensitive, is independent of divalent cations, does not occur via the leukocyte integrin CD11b/CD18, and is not affected by galactose-containing carbohydrates. Organisms bound via HMW proteins remain largely extracellular and viable. Like FHA of Bordetella organisms, HMW proteins mediate binding of NT H. influenzae to macrophages. However, unlike the interaction determined by FHA, this interaction is characteristically one of adhesion and requires additional serum opsonization for efficient killing of bacteria by macrophages.

Citations

Apr 10, 2010·Medical Microbiology and Immunology·Stephanie SchielkeOliver Kurzai
Sep 15, 2001·FEMS Microbiology Letters·J E CraigN J High
Feb 1, 1996·Clinical Molecular Pathology·S SethiK L Klingman
Sep 22, 2015·Journal of Molecular Biology·Julia L E WillettChristopher S Hayes
Mar 22, 2006·The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society·Paul WebsterJoseph W St Geme
Oct 17, 2012·Infection and Immunity·Forrest K RaffelKevin M Mason
Apr 15, 2016·Acta Parasitologica·Darko DavitkovZoran Stanimirovic
Jun 10, 1998·Microbiology and Molecular Biology Reviews : MMBR·A R FoxwellA W Cripps

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