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Related Experiment Videos

PAM, a novel plasminogen-binding protein from Streptococcus pyogenes

A Berge1, U Sjöbring

  • 1Department of Medical and Physiological Chemistry, Lund University, Sweden.

The Journal of Biological Chemistry
|December 5, 1993
PubMed
Summary

Group A streptococci bind plasminogen via M-like proteins, aiding invasion. Researchers identified a novel plasminogen-binding protein, PAM, linked to M proteins, revealing a new virulence mechanism.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Group A streptococci possess M or M-like proteins that bind plasma proteins.
  • This binding may facilitate bacterial invasion and virulence.

Purpose of the Study:

  • To investigate if M or M-like proteins mediate plasminogen binding in Group A streptococci.
  • To identify and characterize the specific protein responsible for plasminogen binding.

Main Methods:

  • Acid extraction of proteins from a M53 streptococcal isolate.
  • Polymerase chain reaction (PCR) using conserved M protein gene sequences.
  • Cloning and expression of a gene fragment in Escherichia coli.
  • Nucleotide sequencing and protein analysis.

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Main Results:

  • A 42-kDa plasminogen-binding protein was extracted from M53 streptococci.
  • A gene fragment encoding a 43-kDa plasminogen-binding protein (PAM) was identified and expressed.
  • PAM shares homology with M proteins, with the binding domain in its amino-terminal third.
  • Bound plasminogen could be activated by streptokinase.

Conclusions:

  • The M protein family is diverse, with PAM representing a new member.
  • PAM contributes to Group A streptococci virulence through plasminogen binding and activation.