Related Experiment Video

Updated: Jun 14, 2026

A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes
07:59

A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes

Published on: March 25, 2014

Antigenic group II chaperonin in Methanobrevibacter oralis may cross-react with human chaperonin CCT

K Yamabe1, H Maeda, S Kokeguchi

  • 1Department of Pathophysiology-Periodontal Science, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, 2-5-1 Shikata-cho, Okayama, Japan.

Molecular Oral Microbiology
|March 25, 2010
PubMed

Insights

Chaperonin subunits from the oral archaeon Methanobrevibacter oralis were found to be antigenic. These molecules were recognized by periodontitis patients

Area of Science:

  • Microbiology
  • Immunology
  • Oral Health

Background:

  • Methanobrevibacter oralis is frequently found in severe periodontitis lesions.
  • The specific pathogenic mechanisms of M. oralis are not fully understood.
  • Chaperonins are essential proteins involved in protein folding and cellular stress responses.

Purpose of the Study:

  • To isolate and characterize group II chaperonin subunits from M. oralis.
  • To investigate the antigenicity of these M. oralis chaperonin subunits.
  • To explore potential cross-reactivity with human chaperonins.

Main Methods:

  • Genes for two chaperonin subunits (Cpn-1 and Cpn-2) were cloned from M. oralis.
  • Recombinant Cpn-1 and Cpn-2 proteins were produced.
  • Western immunoblotting was used to detect antibody reactivity in sera from periodontitis patients and with anti-human chaperonin antibodies.

Main Results:

  • The M. oralis chaperonin genes (Cpn-1 and Cpn-2) were successfully cloned and characterized.
  • A high percentage of periodontitis patients' sera reacted with recombinant M. oralis chaperonins.
  • Antibodies against human chaperonin CCT subunits cross-reacted with M. oralis chaperonins.

Conclusions:

  • Methanobrevibacter oralis chaperonin subunits are antigenic and recognized by patients with periodontitis.
  • These findings suggest a potential role for M. oralis chaperonins in the immune response during periodontitis.
  • Cross-reactivity with human chaperonins indicates potential molecular mimicry or shared epitopes.

More Related Videos

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin11:17

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Published on: March 10, 2021

Visualizing Methane-Cycling Microbial Dynamics in Coastal Wetlands07:26

Visualizing Methane-Cycling Microbial Dynamics in Coastal Wetlands

Published on: January 31, 2025

Related Concept Videos

Phase II Reactions: Methylation Reactions01:17

Phase II Reactions: Methylation Reactions

Methylation is a phase II biotransformation process involving the attachment of a methyl group to a substrate. Enzymes known as methyltransferases orchestrate this reaction.
The mechanism of methylation unfolds in two stages. The first stage sees a methyltransferase enzyme facilitating the transfer of a methyl group from S-adenosylmethionine (SAM) to the substrate, forming S-adenosylhomocysteine (SAH). The second stage involves further metabolism of SAH into homocysteine, which can be recycled...
Cross-reactivity00:42

Cross-reactivity

Overview
Antigens Involved in Adaptive Immunity01:26

Antigens Involved in Adaptive Immunity

An antigen is any substance the immune system identifies as foreign and potentially harmful to the body, prompting an immune response. Antigens have two functional properties: immunogenicity and reactivity. Immunogenicity is the ability of an antigen to stimulate a specific immune response. At the same time, reactivity describes the antigen's ability to react with the cells and antibodies produced in response to it.
Complete Antigens
Complete antigens possess both immunogenicity and reactivity.
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...