Adherence of multiple serovars of Chlamydia trachomatis to a common receptor on HeLa and McCoy cells is mediated by thermolabile protein(s)

E VRETOU; P. C GOSWAMI; Subir K Bose

doi:10.1099/00221287-135-12-3229

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Adherence of multiple serovars of Chlamydia trachomatis to a common receptor on HeLa and McCoy cells is mediated by thermolabile protein(s)

Journal article

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Adherence of multiple serovars of Chlamydia trachomatis to a common receptor on HeLa and McCoy cells is mediated by thermolabile protein(s)

E VRETOU, P. C GOSWAMI and Subir K Bose

Journal of general microbiology, Vol.135(12), pp.3229-3237

1989

DOI: 10.1099/00221287-135-12-3229

PMID: 2636258

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Abstract

Several aspects of the adherence of purified elementary bodies (EB) of Chlamydia trachomatis to HeLa and to McCoy cells were examined using different techniques, including an ELISA. Serovar-specific, biotinylated monoclonal antibodies were used to detect cell-bound chlamy-diae. In addition, purified chlamydiae were biotinylated and their adherence properties were studied. The assays were done at 4°C to exclude the energy-dependent internalization of the cell-bound EB and host-cell membrane recycling that occur at 37°C. Saturation kinetics were routinely observed at 4°C, and the rate of adherence remained linear for approximately 60 min. Lineweaver-Burk analysis of the kinetics data showed that adherence of any one serovar was competitively inhibited by other serovars of C. trachomatis. This competition for the same receptor on the two alternative hosts, HeLa and McCoy, was also seen when the adherence assays were done at 37°C in the presence of sodium azide, an energy poison that inhibits endocytosis of cell-bound chlamydiae. Chlamydiae exposed to 56°C for 5 min, or treated with low doses of trypsin, failed to exhibit competitive inhibition, having suffered considerable loss of the ability to adhere to host-cells. These data suggest that heat- and trypsin-labile chlamydial moieties participate in the adherence reaction, and that oculo-genital serovars of C. trachomatis, including that of lymphogranuloma venereum, attach to the same receptor on the host-cell membrane.

Bacteriology

Microbiology

Fundamental and applied biological sciences. Psychology

Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains

Biological and medical sciences

Details

Title: Subtitle: Adherence of multiple serovars of Chlamydia trachomatis to a common receptor on HeLa and McCoy cells is mediated by thermolabile protein(s)
Creators: E VRETOU - St. Louis univ. school medicine, dep. microbiology, St. Louis MO 63104, United States
P. C GOSWAMI - St. Louis univ. school medicine, dep. microbiology, St. Louis MO 63104, United States
Subir K Bose - St. Louis univ. school medicine, dep. microbiology, St. Louis MO 63104, United States
Resource Type: Journal article
Publication Details: Journal of general microbiology, Vol.135(12), pp.3229-3237
Publisher: Cambridge University Press; London; New York, NY
DOI: 10.1099/00221287-135-12-3229
PMID: 2636258
ISSN: 0022-1287
eISSN: 1465-2080
Language: English
Date published: 1989
Academic Unit: Radiation Oncology
Record Identifier: 9984047693202771

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