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Role of fibronectin-binding MSCRAMMs in bacterial adherence and entry into mammalian cells

D Joh1, E R Wann, B Kreikemeyer

  • 1Center for Extracellular Matrix Biology, Albert B. Alkek Institute of Biosciences and Technology, Texas A&M University System, Houston 77030, USA.

Insights

Microbial Surface Components Recognizing Adhesive Matrix Molecules (MSCRAMMs) bind fibronectin (FN), aiding bacterial adherence and invasion. This interaction involves unique structural repeats and a proposed "sandwich model" with host cell integrins.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Bacterial infections often begin with microbial adherence to host tissues.
  • Adhesins, specific bacterial surface structures, mediate this interaction with host components.
  • Microbial Surface Components Recognizing Adhesive Matrix Molecules (MSCRAMMs) are key adhesins that bind fibronectin (FN).

Purpose of the Study:

  • To review the role of FN-binding MSCRAMMs in bacterial adherence and invasion.
  • To discuss the structure and ligand-binding mechanism of these MSCRAMMs.
  • To explore the proposed "sandwich model" of bacterial entry involving FN and host cell integrins.

Main Methods:

  • Review of existing literature on MSCRAMMs, fibronectin binding, and bacterial invasion.
  • Analysis of structural data for FN-binding MSCRAMMs.
  • Discussion of proposed models for bacterial-host cell interactions.

Main Results:

  • FN-binding MSCRAMMs from staphylococci and streptococci share structural similarities.
  • Their ligand-binding domain features tandem repeats that bind the N-terminal region of FN.
  • These repeat units are unstructured and undergo conformational changes upon FN binding.

Conclusions:

  • FN-MSCRAMM interaction is crucial for bacterial virulence and adherence.
  • FN mediates bacterial entry into non-phagocytic cells via a proposed "sandwich model" with integrins.
  • Further research is needed to fully elucidate the mechanisms of bacterial invasion involving FN and integrins.

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