The Immunochemistry of Peptidoglycan: Antibodies against a Synthetic Immunogen Cross‐Reacting with Peptidoglycan

Karl H. Schleifer, Peter H. Seidl

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

Abstract

A pentapeptide, Gly‐l‐Ala‐l‐Ala‐d‐Ala‐d‐Ala, was synthesized and covalently linked with its free amino group to human serum albumin. Immunization of rabbits with this albumin‐peptide conjugate yielded antisera containing predominantly antibodies directed against the peptide. By means of inhibition studies with various amino‐aicd derivatives and related peptides, it was demonstrated that the antibodies are directed against the C‐terminal portion of the pentapeptide and that d‐alanyl‐d‐alanine is the immunodominant site of the antigen. These antibodies showed also a specific cross‐reaction with solubilized peptidoglycan containing peptide subunits with C‐terminal d‐alanyl‐d‐alanine and with another albumin‐peptide conjugate carrying Gly‐γ‐d‐Glu‐l‐Ala‐d‐Ala‐d‐Ala pentapeptide residues. These albumin‐peptide conjugates also reacted with rabbit antisera of Streptococcus group‐A‐variant which contain antibodies directed against the peptide moiety of the peptidoglycan. Double‐gel diffusion studies with antiserum to Streptococcus group‐A‐variant or to albumin‐peptide conjugate as antibody source and albumin‐peptide‐conjugate and a soluble high molecular fraction of peptidoglycan as antigens yielded precipitin lines which completely fused. This indicates that these antigens have identical determinant groups with respect to the antisera employed.

Original languageEnglish
Pages (from-to)509-519
Number of pages11
JournalEuropean Journal of Biochemistry
Volume43
Issue number3
DOIs
StatePublished - Apr 1974
Externally publishedYes

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