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- W2102820146 abstract "The specificity of antibodies directed against the peptidoglycan of gram-negative bacteria was studied. The peptidoglycans of Proteus vulgaris, Esclierichia colt, Moraxella glucidolytica, Neisseria per/lava, give identical precipitin reactions. By means of inhibition studies with various peptidoglycan subunits and synthetic peptides, it was shown that the antibodies are essentially directed against the peptide moiety of the peptidoglycan: l-Ala-d-G1u 1-(l)-mesoA2pm-(l)-d-Ala, that the peptide reacts better with antibodies when it is not cross-linked, and that the C-terminal portion -meso-A2pm-d-Ala of the peptide is immunodominant. These results explain the immunological identity of the peptidoglycans of gram-negative bacteria, which possess the same peptide subunit. Only weak cross-reactivity was observed with the peptidoglycans of grain-positive bacteria (Streptococcus faecium, Micrococcus lysodeikticus, Corynebacterium poinse ttiae) where mesodiaminopimelic acid is replaced by l-lysine pr l-homoserine. However, the peptidoglycan of Bacillus megaterium which possesses the same peptide subunit as gram-negative bacteria, gives only a reaction of partial identity with these bacteria. This result suggests the presence on the peptidoglycan of gram-negative bacteria, of other undefined antigenic determinants" @default.
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- W2102820146 date "1976-06-01" @default.
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- W2102820146 title "Immunochemical Study of the Peptidoglycan of Gram-Negative Bacteria" @default.
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- W2102820146 doi "https://doi.org/10.1111/j.1432-1033.1976.tb10427.x" @default.
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