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 article

2 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

Fingerprint

IgA-specific serine endopeptidase
Hinges
Immunoglobulin A
Amino Acid Sequence
Amino Acids
Antibodies
Threonine
Streptococcus
Proline
Peptides
Mutation

Keywords

  • Haemophilus influenzae
  • Neisseria meningitidis
  • Streptococcus pneumoniae

Cite this

@article{63dbab2d1ed64f689b0866837104e41e,
title = "Amino acid sequence requirements in the human IgA1 hinge for cleavage by streptococcal IgA1 proteases",
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.",
keywords = "Haemophilus influenzae, Neisseria meningitidis, Streptococcus pneumoniae",
author = "Senior, {B. W.} and Batten, {M. R.} and M. Kilian and Woof, {J. M.}",
year = "2002",
month = "8",
doi = "10.1042/BST0300516",
language = "English",
volume = "30",
pages = "516--518",
journal = "Biochemical Society Transactions",
issn = "0300-5127",
publisher = "Portland Press",
number = "4",

}

Amino acid sequence requirements in the human IgA1 hinge for cleavage by streptococcal IgA1 proteases. / Senior, B. W.; Batten, M. R.; Kilian, M.; Woof, J. M.

In: Biochemical Society Transactions, Vol. 30, No. 4, 08.2002, p. 516-518.

Research output: Contribution to journalConference article

TY - JOUR

T1 - Amino acid sequence requirements in the human IgA1 hinge for cleavage by streptococcal IgA1 proteases

AU - Senior, B. W.

AU - Batten, M. R.

AU - Kilian, M.

AU - Woof, J. M.

PY - 2002/8

Y1 - 2002/8

N2 - 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.

AB - 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.

KW - Haemophilus influenzae

KW - Neisseria meningitidis

KW - Streptococcus pneumoniae

UR - http://www.scopus.com/inward/record.url?scp=0036670512&partnerID=8YFLogxK

U2 - 10.1042/BST0300516

DO - 10.1042/BST0300516

M3 - Conference article

VL - 30

SP - 516

EP - 518

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

SN - 0300-5127

IS - 4

ER -