PA-I AND PA-II LECTIN INTERACTIONS WITH THE ABO(H)-BLOOD AND P-BLOOD GROUP GLYCOSPHINGOLIPID ANTIGENS MAY CONTRIBUTE TO THE BROAD-SPECTRUM ADHERENCE OF PSEUDOMONAS-AERUGINOSA TO HUMAN TISSUES IN SECONDARY INFECTIONS
N. Gilboagarber et al., PA-I AND PA-II LECTIN INTERACTIONS WITH THE ABO(H)-BLOOD AND P-BLOOD GROUP GLYCOSPHINGOLIPID ANTIGENS MAY CONTRIBUTE TO THE BROAD-SPECTRUM ADHERENCE OF PSEUDOMONAS-AERUGINOSA TO HUMAN TISSUES IN SECONDARY INFECTIONS, Glycoconjugate journal, 11(5), 1994, pp. 414-417
Pseudomonas aeruginosa may cause serious infections in most human tiss
ues/organs. Its adherence to them is mediated by a battery of adhesins
including the PA-I and PA-II lectins, which are produced in this bact
erium in high quantities. PA-I binds to the D-galactose of the erythro
cyte glycosphingolipids exhibiting highest affinities for B and P-k (f
ollowed by P-1) antigens, while PA-II preferentially binds to the L-fu
cose of H, A and B antigens. Intact P. aeruginosa cells also exhibit a
clear P-k and P-1 over p preference. Such affinities for the most com
mon human ABH and P system antigens may underlie the widespread tissue
infectivity and pathogenicity of this bacterium.