Some pathogenic bacteria have been demonstrated to secrete specific IgA1-proteases, the enzymes cleaving the molecules of the first subclass of human immunoglobulin (IgA1) in the single point from the hinge with the formation of Fab- and Fc-fragments. Cleavage generally deprives immunoglobulins having defense properties and the enzymes are considered as pathogenic factors. How to determine the activity, purification, and the promises of use of IgA-proteases is described. Whether inactivated meningococcal IgA1-protease as a vaccine against any of the five (A, B, C, Y, W135) serotypes of pathogenic meningococci is discussed.
Download full-text PDF |
Source |
|---|
Publication Analysis
Top Keywords
Similar Publications
Protective Antimicrobial Effect of the Potential Vaccine Created on the Basis of the Structure of the IgA1 Protease from .
Vaccines (Basel)
November 2024
Laboratory of Proteolytic Enzyme Chemistry, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, 117997 Moscow, Russia.
IgA1 protease is one of the virulence factors of , and other pathogens causing bacterial meningitis. The aim of this research is to create recombinant proteins based on fragments of the mature IgA1 protease A-P from serogroup B strain H44/76. These proteins are potential components of an antimeningococcal vaccine for protection against infections caused by pathogenic strains of and other bacteria producing serine-type IgA1 proteases.
View Article and Find Full Text PDFRole of IgA1 protease-producing bacteria in SARS-CoV-2 infection and transmission: a hypothesis.
mBio
October 2024
Department of Microbiology, Heersink School of Medicine, University of Alabama at Birmingham, Birmingham, Alabama, USA.
Secretory (S) IgA antibodies against severe acute respiratory syndrome (SARS)-CoV-2 are induced in saliva and upper respiratory tract (URT) secretions by natural infection and may be critical in determining the outcome of initial infection. Secretory IgA1 (SIgA1) is the predominant isotype of antibodies in these secretions. Neutralization of SARS-CoV-2 is most effectively accomplished by polymeric antibodies such as SIgA.
View Article and Find Full Text PDFSubstitutions in the nonactive site of the passenger domain on the activity of immunoglobulin A1 protease.
Infect Immun
August 2024
Department of Medical Laboratory Science, College of Medical Science and Technology, I-Shou University, Kaohsiung, Taiwan.
Immunoglobulin A1 (IgA1) protease is a critical virulence factor of that facilitates bacterial mucosal infection. This study investigates the effect of gene polymorphism on the enzymatic activity of IgA1 protease. The IgA1 protease activity was examined in the Rd KW20 strain and 51 isolates.
View Article and Find Full Text PDFCorrection to: Specific Antibodies to the Fragments of Meningococcal IgA1 Protease during the Formation of Immunity to Bacterial Infections.
Bull Exp Biol Med
September 2022
M. M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Specific Antibodies to the Fragments of Meningococcal IgA1 Protease during the Formation of Immunity to Bacterial Infections.
Bull Exp Biol Med
August 2022
M. M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
The features of individual fragments of IgA1 protease of Neisseria meningitidis serogroup B during the formation of immunity to bacterial infections in animals and humans were studied. The antibodies to the immunogenic regions of the studied proteins are also detected in mice infected with some bacterial pathogens and in humans with bacterial meningitis. A region of IgA1 protease was identified that is not capable of producing antibodies during immunization of animals, but that detects homologous antibodies in the blood of humans and animals recovered from bacterial infections.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!