Intermediate and C-terminal regions of leptospiral adhesin Lsa66 are responsible for binding with plasminogen and

Rosane Oliveira1,2, Renan F Domingos1,2, Zenaide M de Morais3

  • 1Interunidades em Biotecnologia, Instituto de Ciências Biomédicas, USP, Avenida Prof. Lineu Prestes, 1730, 05508-900 São Paulo, SP, Brazil.

Insights

Researchers studied the Lsa66 protein in Leptospira bacteria. They found specific regions of Lsa66 bind to host components and plasminogen, suggesting a role in infection.

Area of Science:

  • Microbiology
  • Infectious Diseases
  • Bacterial Pathogenesis

Background:

  • Leptospirosis is a global zoonotic disease impacting human and animal health.
  • The leptospiral adhesin Lsa66 binds extracellular matrix (ECM) and plasminogen (PLG).

Purpose of the Study:

  • To clone, express, purify, and characterize three fragments of the Lsa66 protein.
  • To evaluate the binding capabilities of Lsa66 fragments to ECM components and PLG.
  • To identify immune epitopes on Lsa66 recognized by antibodies in leptospirosis patients.

Main Methods:

  • Cloning and expression of N-terminal, intermediate, and C-terminal Lsa66 fragments in Escherichia coli.
  • Purification of recombinant fragments using metal-charged chromatography.
  • Assessment of fragment binding to ECM proteins (laminin, fibronectin) and PLG.
  • Immunological detection of epitopes using sera from leptospirosis-positive individuals.

Main Results:

  • The intermediate Lsa66 fragment bound to laminin, plasma fibronectin, and PLG.
  • The C-terminal fragment showed binding to laminin.
  • Immune epitopes recognized by patient antibodies were localized to the N-terminal and intermediate fragments.

Conclusions:

  • Lsa66 is expressed during Leptospira infection.
  • Specific regions of Lsa66 mediate binding to host factors and PLG.
  • Lsa66 likely plays a significant role in the pathogenesis of leptospirosis.

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