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Monoclonal antibodies against three different enterobacterial outer membrane proteins
Author(s) -
HENRIKSEN ARNE Z.,
MÉLAND JOHAN A.,
BRAKSTAD ODD G.
Publication year - 1989
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.1699-0463.1989.tb00831.x
Subject(s) - microbiology and biotechnology , epitope , monoclonal antibody , enterobacteriaceae , bacilli , bacterial outer membrane , biology , proteus mirabilis , bacteria , escherichia coli , salmonella , antibody , biochemistry , immunology , staphylococcus aureus , genetics , gene
BALB/c mice were immunized with whole‐cells of Escherichia coli 055:B5 or Proteus mirabilis NCTC 60 to produce broadly cross‐reacting monoclonal antibodies (MAbs) against outer membrane (OM) proteins. A total of 10 anti‐OM MAbs of the IgG class were selected. These included 5 MAbs against the heat‐modifiable (Hm) protein, 3 against the peptidoglycan‐associated lipoprotein (PALp), and 2 against Braun's lipoprotein (BLp). Based on competition ELISA, the MAbs defined 2 Hm protein binding sites (Hm I and Hm II), 2 PALp sites (PALp I and PALp II), and one BLp site (BLp I). The MAbs showed broad cross‐reactivity against 74 strains of 10 different genera of the Enterobacteriaceae. Non‐cross‐reacting enteric bacilli occurred only among bacteria of the genera Salmonella, Proteus , and Providentia. The results revealed that Proteus and Providentia strains differed from other enteric bacilli with regard to BLp synthesis or specificity. A panel of 30 non‐enteric Gram‐negative bacteria did not cross‐react. Testing of MAb binding to bacteria showed that a part of the BLp I, PALp I, and PALp II sites was immunoaccessible in intact homologous bacteria, and that the Hm I and Hm II epitopes were inaccessible. The MAbs should facilitate studies of structure and immunobiological function of enterobacterial OM proteins and should have a potential as immunodiagnostic reagents.