Amino acid sequence requirements in the human IgA1 hinge for cleavage by streptococcal IgA1 proteases

B. W. Senior, M. R. Batten, M. Kilian, J. M. Woof

Research output: Contribution to journalConference articlepeer-review

3 Citations (Scopus)

Abstract

All the IgA1 proteases of the different pathogenic species of Streptococcus cleave the hinge of the α chain of human IgA1 only at one proline-threonine peptide bond. In order to study the importance of these amino acids for cleavage, several hinge mutant recombinant IgA1 antibodies were constructed. The mutations were found to be without major effect upon the structure or functional abilities of the antibodies. However, they had a major effect upon their sensitivity to cleavage by some of the IgA1 proteases.

Original languageEnglish
Pages (from-to)516-518
Number of pages3
JournalBiochemical Society Transactions
Volume30
Issue number4
DOIs
Publication statusPublished - Aug 2002

Keywords

  • Haemophilus influenzae
  • Neisseria meningitidis
  • Streptococcus pneumoniae

ASJC Scopus subject areas

  • Biochemistry

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