Characterization of the chaperonin GroEL in Mycoplasma gallisepticum

Lei Tan1, Meirong Hu, Shengqing Yu

  • 1Department of Avian Diseases, Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, No.518, Ziyue Road, Minhang District, Shanghai, 200241, People's Republic of China.

Archives of Microbiology
|October 12, 2014
PubMed

Insights

Mycoplasma gallisepticum (MG) heat shock protein GroEL was identified as a protective antigen. This chaperone protein shows potential as a novel vaccine candidate for poultry respiratory disease.

Area of Science:

  • Veterinary immunology
  • Molecular biology
  • Poultry pathology

Background:

  • Mycoplasma gallisepticum (MG) causes chronic respiratory disease in poultry.
  • Identifying novel antigens is crucial for developing effective vaccines.

Purpose of the Study:

  • To identify antigenic proteins from the MG membrane.
  • To characterize the biological function and potential as a vaccine candidate of MG GroEL.

Main Methods:

  • Two-dimensional gel electrophoresis (2-DE), Western blot, and MALDI-TOF-MS were used to identify antigenic proteins.
  • Recombinant MG GroEL was expressed in E. coli and its ATPase and refolding activities were assessed.
  • Complement-dependent bactericidal assays were performed using antisera against MG rGroEL.

Main Results:

  • Several antigenic proteins were identified, including heat shock protein GroEL.
  • Recombinant MG GroEL exhibited ATPase activity and aided in refolding another protein (PrpC).
  • Antisera against MG rGroEL demonstrated significant bactericidal effects against MG.

Conclusions:

  • MG GroEL is a protective antigen with potential as a novel vaccine candidate.
  • This study provides the first report on the biological characterization of chaperone GroEL in MG.
  • Targeting MG GroEL could lead to new strategies for controlling poultry respiratory disease.

Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
14.6K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

14.1K
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
739
Gram-negative Bacterial Protein Secretion Systems01:17

Gram-negative Bacterial Protein Secretion Systems

Gram-negative bacteria utilize sophisticated protein secretion systems to transport proteins across their double-membrane envelope into the extracellular environment or host cells. Based on their mechanism of action, these systems are classified into one-step and two-step pathways.One-Step Secretion Systems (Types I, III, IV, and VI)One-step secretion systems bypass the periplasm entirely, forming a continuous channel that spans both the inner and outer membranes:Type I Secretion System (T1SS):...
1.6K
Bacterial Phylum Chlamydiae01:29

Bacterial Phylum Chlamydiae

The phylum Chlamydiae or Chlamydiota is composed of a single order, Chlamydiales. This phylum consists entirely of obligate intracellular parasites that infect eukaryotic hosts. While human pathogens within this group have been studied extensively, the phylum encompasses many species capable of interacting with various eukaryotic organisms. Members of Chlamydiae are typically small cocci, approximately 0.5 μm in diameter, and exhibit a distinctive developmental cycle. As is characteristic...
826
Archaeal Cell Wall01:29

Archaeal Cell Wall

Archaeal cell walls are structurally and compositionally distinct from their bacterial counterparts, lacking the characteristic peptidoglycan layer found in most bacteria. Instead, archaeal cell walls exhibit remarkable diversity, utilizing materials such as pseudomurein, polysaccharides, and proteins to construct their protective outer layers. This structural flexibility is closely tied to archaea's ecological adaptability.S-Layers: The Common Archaeal Cell WallThe S-layer is the most...
1.6K