Cloning and characterization of the genes coding for antigen 85A, 85B and 85C of Mycobacterium avium subsp.

Veerabadran Dheenadhayalan1, Kwang-Soon Shin, Chao-Fu Chang

  • 1Department of Population Medicine and Diagnostic Sciences, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA.

Insights

Three antigen 85 genes from Mycobacterium avium subsp. paratuberculosis were sequenced, showing high homology with other mycobacterial species. Conserved fibronectin-binding regions were identified in these secreted proteins.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Genetics

Background:

  • The antigen 85 complex is a group of secreted proteins in mycobacteria.
  • These proteins play roles in cell wall synthesis and immune response.
  • Understanding these proteins in Mycobacterium avium subsp. paratuberculosis is crucial for diagnostics and therapeutics.

Purpose of the Study:

  • To clone, sequence, and analyze three antigen 85 genes (A, B, and C) from Mycobacterium avium subsp. paratuberculosis.
  • To compare these sequences with those from other mycobacterial species.
  • To investigate conserved regions potentially involved in fibronectin binding.

Main Methods:

  • Gene cloning and DNA sequencing of antigen 85-A, B, and C.
  • Bioinformatic analysis including multiple sequence alignment and homology analysis.
  • Identification of conserved protein regions.

Main Results:

  • The complete sequences of the three antigen 85 proteins from M. avium subsp. paratuberculosis were determined.
  • These sequences exhibited 99% homology with M. avium 85-complex proteins and high similarity to other mycobacterial species.
  • Variations were localized to specific amino acid positions across different mycobacterial 85-complex proteins.
  • Three conserved regions, known for fibronectin binding in other mycobacteria, were identified in the N-terminal regions of M. avium subsp. paratuberculosis 85A, B, and C.

Conclusions:

  • The antigen 85 proteins of M. avium subsp. paratuberculosis share significant sequence homology with their counterparts in other mycobacteria.
  • The identified conserved N-terminal regions suggest a conserved function in fibronectin binding across species.
  • These findings contribute to understanding the molecular characteristics of M. avium subsp. paratuberculosis and potential targets for intervention.

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