Open AccessHaemagglutinating activity of Campylobacter pylori
Author(s) -
Huang Jinzhou,
Smyth Cyril J.,
Kennedy Nicholas P.,
Arbuthnott John P.,
Keeling P.W.Napoleon
Publication year - 1988
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1988.tb03159.x
Subject(s) - hemagglutination , agglutination (biology) , microbiology and biotechnology , biology , campylobacter , protease , neuraminidase , horse , virology , biochemistry , bacteria , antigen , virus , immunology , enzyme , paleontology , genetics
Thirty‐one isolates of Campylobacter pylori , screened for their ability to agglutinate a panel of erythrocyte species, could be divided into two phenotypic groups on the basis of their ability to agglutinate human A and O erythrocytes, a property which correlated strongly with their ability to agglutinate horse and cat erythrocytes. Isolates which agglutinated human red blood cells exhibited a broad‐spectrum haemagglutination profile on other red blood cells including dog, goat, guinea‐pig, ox, rat and sheep erythrocytes. Agglutination dog, guinea‐pig, horse and human erythrocytes by C. pylori was mannose‐resistant. Haemagglutination was not inhibited by other saccharides tested nor by two glycoproteins or serine. The bacterial ligand was protease‐ and heat‐sensitive. Neither protease nor neuraminidase treatment of erythrocytes prevented agglutination.