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. 1980 Jul;143(1):205–211. doi: 10.1128/jb.143.1.205-211.1980

Agglutination of human erythrocytes by Fusobacterium nucleatum: factors influencing hemagglutination and some characteristics of the agglutinin.

P Dehazya, R S Coles Jr
PMCID: PMC294211  PMID: 6995428

Abstract

Various aspects of agglutination of human erythrocytes by fusobacterium nucleatum were examined. Titration experiments done in buffered saline at pH 6 to 10 showed the same agglutination endpoint. The presence of high concentrations of NaCl in reaction mixtures did not alter titers, but KCl in concentrations of 0.5 to 3.6 M increased titers twofold. The agglutinin was inactivated by heat, acid, alkali, 5% Formalin, and the proteolytic enzyme subtilopeptidase A and therefore appeared to be a protein. Treatment of bacterial cells with 2-mercaptoethanol had no effect. Hemagglutination inhibition experiments revealed that arginine and other compounds containing a guanido group as part of their structure were inhibitory at low concentrations. Various hexoses, some hexose derivatives, and most common metal ions, when added to bacterium-erythrocyte mixtures, had no effect. The binding of dansyl-L-arginine to bacteria, but not erythrocytes, was demonstrable by ultraviolet fluorescence microscopy.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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