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. 1983 Jun;40(3):1060–1067. doi: 10.1128/iai.40.3.1060-1067.1983

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

S K Bose, G B Smith, R G Paul
PMCID: PMC348158  PMID: 6687878

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.

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Selected References

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  1. Beachey E. H. Bacterial adherence: adhesin-receptor interactions mediating the attachment of bacteria to mucosal surface. J Infect Dis. 1981 Mar;143(3):325–345. doi: 10.1093/infdis/143.3.325. [DOI] [PubMed] [Google Scholar]
  2. Bhavanandan V. P., Katlic A. W. The interaction of wheat germ agglutinin with sialoglycoproteins. The role of sialic acid. J Biol Chem. 1979 May 25;254(10):4000–4008. [PubMed] [Google Scholar]
  3. Bose S. K., Mudd R. L. Modulation of bacterial association to HeLa cell cultures by cell density and by chlamydial infection. Infect Immun. 1981 Oct;34(1):154–159. doi: 10.1128/iai.34.1.154-159.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bose S. K., Paul R. G. Purification of Chlamydia trachomatis lymphogranuloma venereum elementary bodies and their interaction with HeLa cells. J Gen Microbiol. 1982 Jun;128(6):1371–1379. doi: 10.1099/00221287-128-6-1371. [DOI] [PubMed] [Google Scholar]
  5. Byrne G. I. Kinetics of phagocytosis of Chlamydia psittaci by mouse fibroblasts (L cells): separation of the attachment and ingestion stages. Infect Immun. 1978 Feb;19(2):607–612. doi: 10.1128/iai.19.2.607-612.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Byrne G. I., Moulder J. W. Parasite-specified phagocytosis of Chlamydia psittaci and Chlamydia trachomatis by L and HeLa cells. Infect Immun. 1978 Feb;19(2):598–606. doi: 10.1128/iai.19.2.598-606.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Byrne G. I. Requirements for ingestion of Chlamydia psittaci by mouse fibroblasts (L cells). Infect Immun. 1976 Sep;14(3):645–651. doi: 10.1128/iai.14.3.645-651.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Chen T. R. In situ detection of mycoplasma contamination in cell cultures by fluorescent Hoechst 33258 stain. Exp Cell Res. 1977 Feb;104(2):255–262. doi: 10.1016/0014-4827(77)90089-1. [DOI] [PubMed] [Google Scholar]
  9. Hatch T. P., Vance D. W., Jr, Al-Hossainy E. Attachment of Chlamydia psittaci to formaldehyde-fixed and unfixed L cells. J Gen Microbiol. 1981 Aug;125(2):273–283. doi: 10.1099/00221287-125-2-273. [DOI] [PubMed] [Google Scholar]
  10. Kuo C. C., Wang S. P., Grayston J. T., Alexander E. R. TRIC type K, a new immunologic type of Chlamydia trachomatis. J Immunol. 1974 Aug;113(2):591–596. [PubMed] [Google Scholar]
  11. Kuo C. C., Wang S. P., Grayston J. T. Effect of polycations, polyanions and neuraminidase on the infectivity of trachoma-inclusin conjunctivitis and lymphogranuloma venereum organisms HeLa cells: sialic acid residues as possible receptors for trachoma-inclusion conjunction. Infect Immun. 1973 Jul;8(1):74–79. doi: 10.1128/iai.8.1.74-79.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kuo C., Wang S., Grayston J. T. Differentiation of TRIC and LGV organisms based on enhancement of infectivity by DEAE-dextran in cell culture. J Infect Dis. 1972 Mar;125(3):313–317. doi: 10.1093/infdis/125.3.313. [DOI] [PubMed] [Google Scholar]
  13. LIEBHABER H., TAKEMOTO K. K. Alteration plaque morphology of EMC virus with polycations. Virology. 1961 Aug;14:502–504. doi: 10.1016/0042-6822(61)90349-x. [DOI] [PubMed] [Google Scholar]
  14. Lee C. K. Interaction between a trachoma strain of Chlamydia trachomatis and mouse fibroblasts (McCoy cells) in the absence of centrifugation. Infect Immun. 1981 Feb;31(2):584–591. doi: 10.1128/iai.31.2.584-591.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Levy N. J. Wheat germ agglutinin blockage of chlamydial attachment sites: antagonism by N-acetyl-D-glucosamine. Infect Immun. 1979 Sep;25(3):946–953. doi: 10.1128/iai.25.3.946-953.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Monsigny M., Roche A. C., Sene C., Maget-Dana R., Delmotte F. Sugar-lectin interactions: how does wheat-germ agglutinin bind sialoglycoconjugates? Eur J Biochem. 1980 Feb;104(1):147–153. doi: 10.1111/j.1432-1033.1980.tb04410.x. [DOI] [PubMed] [Google Scholar]
  17. Peters B. P., Ebisu S., Goldstein I. J., Flashner M. Interaction of wheat germ agglutinin with sialic acid. Biochemistry. 1979 Nov 27;18(24):5505–5511. doi: 10.1021/bi00591a038. [DOI] [PubMed] [Google Scholar]
  18. Ripa K. T., Mårdh P. A. Cultivation of Chlamydia trachomatis in cycloheximide-treated mccoy cells. J Clin Microbiol. 1977 Oct;6(4):328–331. doi: 10.1128/jcm.6.4.328-331.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Rota T. R., Nichols R. L. Infection of cell cultures by trachoma agent: enhancement by DEAE-dextran. J Infect Dis. 1971 Oct;124(4):419–421. doi: 10.1093/infdis/124.4.419. [DOI] [PubMed] [Google Scholar]
  20. Salari S. H., Ward M. E. Polypeptide composition of Chlamydia trachomatis. J Gen Microbiol. 1981 Apr;123(2):197–207. doi: 10.1099/00221287-123-2-197. [DOI] [PubMed] [Google Scholar]
  21. Sharon N., Lis H. Lectins: cell-agglutinating and sugar-specific proteins. Science. 1972 Sep 15;177(4053):949–959. doi: 10.1126/science.177.4053.949. [DOI] [PubMed] [Google Scholar]
  22. Stanley P., Carver J. P. Selective loss of wheat germ agglutinin binding to agglutinin-resistant mutants of Chinese hamster ovary cells. Proc Natl Acad Sci U S A. 1977 Nov;74(11):5056–5059. doi: 10.1073/pnas.74.11.5056. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Toyoshima K., Vogt P. K. Enhancement and inhibition of avian sarcoma viruses by polycations and polyanions. Virology. 1969 Jul;38(3):414–426. doi: 10.1016/0042-6822(69)90154-8. [DOI] [PubMed] [Google Scholar]
  24. Wright C. S. Crystallographic elucidation of the saccharide binding mode in wheat germ agglutinin and its biological significance. J Mol Biol. 1980 Aug 15;141(3):267–291. doi: 10.1016/0022-2836(80)90181-3. [DOI] [PubMed] [Google Scholar]

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