POLYMANNOSE O-ANTIGENS OF ESCHERICHIA-COLI, THE BINDING-SITES FOR THE REVERSIBLE ADSORPTION OF BACTERIOPHAGE-T5+ VIA THE L-SHAPED TAIL FIBERS
POLYMANNOSE O-ANTIGENS OF ESCHERICHIA-COLI, THE BINDING-SITES FOR THE REVERSIBLE ADSORPTION OF BACTERIOPHAGE-T5+ VIA THE L-SHAPED TAIL FIBERS
复制标题
DOI:
10.1128/jvi.41.1.222-227.1982
复制
发表时间:
1982-01-01
影响因子:
5.4
通讯作者:
BRAUN, V
中科院分区:
文献类型:
--
作者:
HELLER, K;BRAUN, V
A study of the adsorption kinetics of T5+ and the tail fiber-less mutant hd-2 to lipopolysaccharides of various E. coli strains demonstrated T5+ binding to the O-antigen of the O8 and O9 types. Incorporation of radioactive mannose into the phosphomannose isomerase-deficient strain E. coli F860 O9 pmi allowed the derivation of the number of O-antigens/cell required to increase T5 adsorption. With > 500 O-antigen molecules, acceleration of T5+ adsorption was observed. The highest adsorption rate was obtained when nearly all lipopolysaccharide molecules were substituted with a polymannose O-antigen. Inhibition studies with purified components of an enzymatically degraded lipopolysaccharide of the O8 type showed that among the mannosides tested the smallest unit, the trimannoside, was the strongest inhibitor of T5+ binding. Thus, the reversible preadsorption to the O8 and O9 polymannose antigens increases the rate of infection via the cellular receptor protein encoded by the fhuA (formerly tonA) gene.