This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Bose, S K Articles by Paul, R G Search for Related Content PubMed PubMed Citation Articles by Bose, S K Articles by Paul, R G

 Previous Article  |  Next Article 

Infect Immun. 1983 June; 40(3): 1060-1067

Influence of lectins, hexoses, and neuraminidase on the association of purified elementary bodies of Chlamydia trachomatis UW-31 with HeLa cells.

ABSTRACT

Using highly purified elementary bodies of Chlamydia trachomatis UW-31 (serotype K), we found that HeLa 229 monolayer cultures bound more 32P-labeled chlamydiae after pretreatment with the lectin wheat germ agglutinin. The lectin, on the other hand, inhibited competitively when chlamydial association was assayed in the presence of polycations. The two effects of wheat germ agglutinin were abolished when N-acetylneuraminic acid (NeuNAc)- or N-acetylglucosamine (GlcNAc)-preincubated wheat germ agglutinin was used. Brief exposure of HeLa cells to neuraminidase abolished the ability to bind the elementary bodies, whether or not polycations were present. Furthermore, at 5 degrees C but not at 37 degrees C, NeuNAc, GlcNAc and N-acetylgalactosamine inhibited chlamydial association only in the absence of the polycation DEAE-dextran. The results suggest that NeuNAc residues on the plasma membrane are the principal, but not the only, receptors for this strain of C. trachomatis.

This article has been cited by other articles:

• Vretou, E., Giannikopoulou, P., Psarrou, E. (2001). Polymorphic outer-membrane proteins of Chlamydophila abortus are glycosylated. Microbiology 147: 3303-3310 [Abstract] [Full Text]