Open AccessVi‐deficient and nonfimbriated mutants of Salmonella typhi agglutinate human blood type antigens and are hyperinvasive
Author(s) -
Miyake Masaki,
Zhao Licheng,
Ezaki Takayuki,
Hirose Kenji,
Khan Abdul Quayum,
Kawamura Yoshiaki,
Shima Ryuichiro,
Kamijo Miki,
Masuzawa Toshiyuki,
Yanagihara Yasutake
Publication year - 1998
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.1574-6968.1998.tb12931.x
Subject(s) - mutant , antigen , microbiology and biotechnology , wild type , biology , saccharomyces cerevisiae , salmonella typhi , blood type (non human) , abo blood group system , escherichia coli , yeast , biochemistry , gene , immunology
We generated nonfimbriated mutants from both Vi‐positive and ‐negative Salmonella typhi to analyze the role of type 1 fimbriae and Vi‐antigen in bacterial invasion. A Vi‐defective mutant of S. typhi GIFU 10007‐3 was more invasive than the wild‐type strain GIFU 10007. The wild‐type strain expressing Vi‐antigen did not agglutinate both Saccharomyces cerevisiae and human erythrocytes but Vi‐defective mutants were able to agglutinate S. cerevisiae and human erythrocytes. Nonfimbriated mutants from Vi‐negative GIFU 10007‐3 lost the ability to adhere to S. cerevisiae but still could agglutinate human erythrocytes. The Vi‐negative mutant increased secreted proteins and became 5‐fold more invasive than the wild‐type strain. Nonfimbriated Vi mutants became 50–120‐fold more invasive than the wild‐type GIFU 10007. To determine why nonfimbriated Vi mutants still agglutinate human red blood cells, we searched bacterial proteins that could bind human blood‐type antigens. We finally identified a candidate 37 kDa outer membrane protein that recognized fucosyl‐galactose, a structure common to blood type A, B and H antigens.