Chlamydia-dependent biosynthesis of a heparan sulphate-like compound in eukaryotic cells |
| |
Authors: | Rasmussen-Lathrop S J Koshiyama K Phillips N Stephens R S |
| |
Institution: | The Francis I. Proctor Foundation, University of California, San Francisco, CA 94143, USA.,;Program in Infectious Diseases, School of Public Health, 235 Earl Warren Hall, University of California, Berkeley, CA 94720, USA.,;Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143, USA. |
| |
Abstract: | One hypothesis for the mechanism of chlamydial interaction with its eukaryotic host cell invokes a trimolecular mechanism, whereby a Chlamydia -derived glycosaminoglycan bridges a chlamydial acceptor molecule and a host receptor enabling attachment and invasion. We show that a heparan sulphate-specific monoclonal antibody specifically binds a glycosaminoglycan localized to the surface of the chlamydial organism and effectively neutralizes infectivity of both C. trachomatis and C. pneumoniae . In addition to the ability of this antibody to neutralize infectivity, direct visualization using immunofluorescence demonstrated staining of chlamydial organisms localized to the intracellular vacuole. The chlamydial-associated glycosaminoglycan was specifically labelled with 14C]-glucosamine, and the labelled compound was immunoprecipitated and resolved by gel electrophoresis. The chlamydial-associated glycosaminoglycan is a high-molecular-weight compound similar in size to heparin or heparan sulphate and was sensitive to cleavage by heparan sulphate lyase. These data demonstrate that a glucosamine-containing sulphated polysaccharide is produced within the intracellular vacuole containing chlamydiae and is a target for antibody-mediated neutralization of infectivity. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|