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A conserved domain on enterobacterial porin protein analysed by monoclonal antibody
Author(s) -
HENRIKSEN ARNE Z.,
MÆLAND JOHAN A.
Publication year - 1991
Publication title -
apmis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0903-4641
DOI - 10.1111/j.1699-0463.1991.tb05117.x
Subject(s) - lysozyme , microbiology and biotechnology , lysostaphin , monoclonal antibody , porin , biology , bacterial outer membrane , morganella morganii , peptidoglycan , enterobacteriaceae , salmonella , antigenicity , epitope , cross reactivity , bacteria , antigen , antibody , chemistry , enzyme , escherichia coli , biochemistry , staphylococcus aureus , cross reactions , gene , genetics , immunology
Broadly cross‐reactive monoclonal antibodies (MAbs) against enterobacterial outer membrane (OM) porin (Po) protein were isolated after immunization of BALB/c mice with whole cells of E. coli 055:B5. MAbs (n=6) of the IgG class but of four different isotypes were studied. Based on a competition ELISA, all of the MAbs were directed against one and the same Po protein domain (PoI). The MAbs cross‐reacted with 72 of 74 strains from 10 different genera of the Enterobacteriaceae. One Morganella and one Salmonella strain showed no cross‐reactivity. Also, nine strains of various Neisseria spp. cross‐reacted while 21 strains of various other nonenteric Gram‐negative bacteria showed no cross‐reactivity. The Po I sites were inaccessible in intact homologous bacteria but partially accessible in the OM. Digestion of OM with lysozyme or lysostaphin affected the accessibility of the Po I sites in OMs of various enterobacteria. Lysostaphin strongly enhancefd the immunoaccessibility, whereas lysozyme had lesser effects. The enzymes also affected the binding by Neisseria OMs of the anti‐Po I MAb. The Po I site was immunogenic both in humans and rabbits. The data indicate that Po I is an important Po protein domain, and that the effects of peptidoglycan‐degrading enzymes must be considered in studies of Po protein domains.