Journal Article

Binding of influenza type A viruses to group B <i>Streptococcus</i> and haemagglutination by virus-bound bacteria

Yasuhiro Hosaka, Ikeura Akihiro, Yu-ichi Harada, Kazumichi Kuroda, Hideki Hamayasu, Takashi Suzuki, Kazunari Yamada, Yuji Kawase and Yasuo Suzuki

in Microscopy

Published on behalf of The Japanese Society of Microscopy

Volume 49, issue 6, pages 765-773
Published in print January 2000 | ISSN: 2050-5698
Published online January 2000 | e-ISSN: 2050-5701 | DOI:
Binding of influenza type A viruses to group B Streptococcus and haemagglutination by virus-bound bacteria

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We studied the bindings of human influenza A type viruses to group B Streptococcus (GBS), types la, n, m and IV, of sialic acid (SA)α2-3 linkage, using A/PR/8/34(HlNl) and A;Memphis/l/71(H3N2). The viruses were found to bind to all types of GBS, with the exception of PR/8/34 for GBSIt, and to elute from GBSIa, HI and IV at 37°C, except GBSII. Electron microscopy confirmed these behaviours of the influenza viruses. The virus-binding capability of GBS types seemed to depend on the side chain length of the terminal SA. Treatment of GBSIa, HI and IV, except enzyme-resistant type II, with bacterial neuraminidase resulted in the loss of virus-binding capability of GBS. These findings confirmed that SAcx2-3 linkage of GBS capsules functions as receptor for human influenza viruses [1]. When singular bacteria were prepared from mainly chain-like GBS with sonication, viruses were found to bind to them more efficiently. Untreated and sonicated GBS were both aggregated with high doses of virus. Furthermore, using A/Memphis/ 1/71(H3N2) and GBSII, we found that virus-bound GBS, untreated or sonicated, caused haemagglutination (HA). The morphological evidence that chicken erythrocytes were bridged with virus-bound native GBSII, supporting occurrences of HA, was obtained. Statistical analysis suggested that HA by virus-bound sonicated (singular) GBS was mediated by bacteria bound by at least two or three virus particles.

Keywords: influenza virus; group B Streptococcus (GBS); receptor activity; SEM; sialyl-galactose chain; haemagglutination

Journal Article.  0 words. 

Subjects: Biological Sciences

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