Neuraminidase-dependent hamagglutination of human erythrocytes by human strains of Actinomyces viscosus and Actinomyces naeslundii - PubMed (original) (raw)

Neuraminidase-dependent hamagglutination of human erythrocytes by human strains of Actinomyces viscosus and Actinomyces naeslundii

A H Costello et al. Infect Immun. 1979 Nov.

Abstract

Human A, B, and O erythrocytes (RBC) were agglutinated by many human strains of Actinomyces viscosus and A. naeslundii. At 37 degrees C, these bacterium-mediated hemagglutination reactions required the action of bacterial neuraminidase upon the RBC; however, at 4 degrees C, the requirement for neuraminidase was not as striking. Bacterial cell suspensions which caused hemagglutination at 37 degrees C contained both soluble extracellular and cell-associated neuraminidase activities as shown by enzyme assays using a soluble substrate (i.e., alpha 1-acid glycoprotein). Bacterium-mediated hemagglutination occurred only in the presence of soluble neuraminidase activity, and the rate of hemagglutination could be inhibited by 2-deoxy-2,3-dehydro-N-acetylneuraminic acid, a competitive inhibitor of purified soluble neuraminidase from A. viscosus T14V. Suspensions of bacteria which contained only cell-associated neuraminidase activity were unable to initiate hemagglutination, but they caused immediate hemagglutination when mixed with neuraminidase-treated RBC. All hemagglutination reactions were reversible in the presence of 0.02 M lactose and were abolished by heating (85 degrees C for 30 min) the actinomycete cells but not the RBC. The proposed mechanism of hemagglutination involves two sequential steps: (i) the action of neuraminidase to unmask galactose-containing receptors on the RBC and (ii) the multivalent binding of these receptors by many low-affinity lection sites on the bacterial surface.

PubMed Disclaimer

Similar articles

• Sialidase-enhanced lectin-like mechanism for Actinomyces viscosus and Actinomyces naeslundii hemagglutination.
  Ellen RP, Fillery ED, Chan KH, Grove DA. Ellen RP, et al. Infect Immun. 1980 Feb;27(2):335-43. doi: 10.1128/iai.27.2.335-343.1980. Infect Immun. 1980. PMID: 6769798 Free PMC article.
• Detection and localization of a lectin on Actinomyces viscosus T14V by monoclonal antibodies.
  Cisar JO, Barsumian EL, Curl SH, Vatter AE, Sandberg AL, Siraganian RP. Cisar JO, et al. J Immunol. 1981 Oct;127(4):1318-22. J Immunol. 1981. PMID: 6115881
• Isolation of a neuraminidase gene from Actinomyces viscosus T14V.
  Yeung MK, Fernandez SR. Yeung MK, et al. Appl Environ Microbiol. 1991 Nov;57(11):3062-9. doi: 10.1128/aem.57.11.3062-3069.1991. Appl Environ Microbiol. 1991. PMID: 1781674 Free PMC article.
• [Biological activities of a human dental plaque specimen, and cell walls from Actinomyces viscosus and Actinomyces naeslundii].
  Yamagami H. Yamagami H. Osaka Daigaku Shigaku Zasshi. 1978 Jun;23(1):78-95. Osaka Daigaku Shigaku Zasshi. 1978. PMID: 397329 Review. Japanese. No abstract available.
• Molecular basis of bacterial adhesion in the oral cavity.
  Mergenhagen SE, Sandberg AL, Chassy BM, Brennan MJ, Yeung MK, Donkersloot JA, Cisar JO. Mergenhagen SE, et al. Rev Infect Dis. 1987 Sep-Oct;9 Suppl 5:S467-74. doi: 10.1093/clinids/9.supplement_5.s467. Rev Infect Dis. 1987. PMID: 2891180 Review.

Cited by

• Factors affecting binding of galacto ligands to Actinomyces viscosus lectin.
  Heeb MJ, Marini AM, Gabriel O. Heeb MJ, et al. Infect Immun. 1985 Jan;47(1):61-7. doi: 10.1128/iai.47.1.61-67.1985. Infect Immun. 1985. PMID: 2578122 Free PMC article.
• Role of hydrogen peroxide in competition and cooperation between Streptococcus gordonii and Actinomyces naeslundii.
  Jakubovics NS, Gill SR, Vickerman MM, Kolenbrander PE. Jakubovics NS, et al. FEMS Microbiol Ecol. 2008 Dec;66(3):637-44. doi: 10.1111/j.1574-6941.2008.00585.x. Epub 2008 Sep 9. FEMS Microbiol Ecol. 2008. PMID: 18785881 Free PMC article.
• Specific and nonspecific inhibition of adhesion of oral actinomyces and streptococci to erythrocytes and polystyrene by caseinoglycopeptide derivatives.
  Neeser JR, Chambaz A, Del Vedovo S, Prigent MJ, Guggenheim B. Neeser JR, et al. Infect Immun. 1988 Dec;56(12):3201-8. doi: 10.1128/iai.56.12.3201-3208.1988. Infect Immun. 1988. PMID: 3182077 Free PMC article.
• Isolation and characterization of Actinomyces viscosus mutants defective in binding salivary proline-rich proteins.
  Nesbitt WE, Beem JE, Leung KP, Clark WB. Nesbitt WE, et al. Infect Immun. 1992 Mar;60(3):1095-100. doi: 10.1128/iai.60.3.1095-1100.1992. Infect Immun. 1992. PMID: 1347286 Free PMC article.
• A 160-kilodalton epithelial cell surface glycoprotein recognized by plant lectins that inhibit the adherence of Actinomyces naeslundii.
  Brennan MJ, Cisar JO, Sandberg AL. Brennan MJ, et al. Infect Immun. 1986 Jun;52(3):840-5. doi: 10.1128/iai.52.3.840-845.1986. Infect Immun. 1986. PMID: 2872166 Free PMC article.

References

1. 1. Proc Natl Acad Sci U S A. 1977 Oct;74(10):4591-4 - PubMed
2. 1. Biochem Biophys Res Commun. 1978 Dec 29;85(4):1551-9 - PubMed
3. 1. Infect Immun. 1978 Sep;21(3):978-88 - PubMed
4. 1. Infect Immun. 1979 May;24(2):523-31 - PubMed
5. 1. J Exp Med. 1977 Nov 1;146(5):1182-94 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources

• Full Text Sources

  • Atypon
  • Europe PubMed Central
  • PubMed Central

• Other Literature Sources

  • The Lens - Patent Citations Database