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Shot-gun phage display mapping of two streptococcal cell-surface proteins.

Authors
  • Jacobsson, K
  • Jonsson, H
  • Lindmark, H
  • Guss, B
  • Lindberg, M
  • Frykberg, L
Type
Published Article
Journal
Microbiological Research
Publisher
Elsevier
Publication Date
Jul 01, 1997
Volume
152
Issue
2
Pages
121–128
Identifiers
PMID: 9265766
Source
Medline
License
Unknown

Abstract

We have used a phage display shot-gun cloning technique to map the binding domains in two cell surface proteins from animal group C streptococci. The proteins, MAG and ZAG, have affinity for alpha (2)-macroglobulin (alpha (2)M), serum albumin and IgG. In this work, parts of cloned i mag and zag genes were randomly cloned into a phagemid vector, and recombinant phages expressing alpha (2)-M- or albumin-binding activity were isolated through panning against immobilized alpha (2)M or albumin. Analysis of the clones revealed two distinct alpha (2)M-binding sites in protein MAG and two slightly overlapping binding sites in protein ZAG. The minimal albumin-binding domain in protein ZAG, as deduced from the affinity selected clones, consisted of 42 amino acids. These results show that the phage display shot-gun cloning is a rapid and convenient way to characterize the binding site(s) in receptor proteins without any prior knowledge of their number, size, and localization.

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