ArticleInfection and immunity1996
A 35-kilodalton protein is a major target of the human immune response to Mycobacterium leprae.
Article in Infection and immunity, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
27 citing papers in PubMed, 61 citations in OpenAlex.
- Review
- Encapsulins: Structure, Properties, and Biotechnological Applications.Biochemistry. Biokhimiia · 2023Review
- Encapsulins.Annual review of biochemistry · 2022Review
- Nanotechnological Applications Based on Bacterial Encapsulins.Nanomaterials (Basel, Switzerland) · 2021Review
- Advances in encapsulin nanocompartment biology and engineering.Biotechnology and bioengineering · 2021Review
- Encapsulins-Bacterial Protein Nanocompartments: Structure, Properties, and Application.Biomolecules · 2020Review
- A standardized production pipeline for high profile targets from Mycobacterium tuberculosis.Proteomics. Clinical applications · 2016Article
- Production of recombinant proteins in Mycobacterium smegmatis for structural and functional studies.Protein science : a publication of the Protein Society · 2015Review
- Enhanced expression of codon optimized Mycobacterium avium subsp. paratuberculosis antigens in Lactobacillus salivarius.Frontiers in cellular and infection microbiology · 2014Article
- No holes barred: invasion of the intestinal mucosa by Mycobacterium avium subsp. paratuberculosis.Infection and immunity · 2013Review
- Gene expression profile and immunological evaluation of unique hypothetical unknown proteins of Mycobacterium leprae by using quantitative real-time PCR.Clinical and vaccine immunology : CVI · 2013Article
- Serodiagnostic potential of Mycobacterium avium MAV2054 and MAV5183 proteins.Clinical and vaccine immunology : CVI · 2013Article
- Leprosy and the human genome.Microbiology and molecular biology reviews : MMBR · 2010Review
- Production and characterization of monoclonal antibodies against a major membrane protein of Mycobacterium avium subsp. paratuberculosis.Clinical and vaccine immunology : CVI · 2007Article
- Rapid expression of Mycobacterium avium subsp. paratuberculosis recombinant proteins for antigen discovery.Clinical and vaccine immunology : CVI · 2007Article
- Expression library immunization confers protection against Mycobacterium avium subsp. paratuberculosis infection.Infection and immunity · 2005Article
- Gamma interferon responses induced by a panel of recombinant and purified mycobacterial antigens in healthy, non-mycobacterium bovis BCG-vaccinated Malawian young adults.Clinical and diagnostic laboratory immunology · 2003Article
- Article
- Human T cell responses to peptides of the Mycobacterium leprae 45-kD serine-rich antigen.Clinical and experimental immunology · 2002Article
- Comparative protective effects of recombinant DNA and Mycobacterium bovis bacille Calmette-Guérin vaccines against M. avium infection.Clinical and experimental immunology · 2001Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The control of leprosy will be facilitated by the identification of major Mycobacterium leprae-specific antigens which mirror the immune response to the organism across the leprosy spectrum. We have investigated the host response to a 35-kDa protein of M. leprae. Recombinant 35-kDa protein purified from Mycobacterium smegmatis resembled the native antigen in the formation of multimeric complexes and binding by monoclonal antibodies and sera from leprosy patients. These properties were not shared by two forms of 35-kDa protein purified from Escherichia coli. The M. smegmatis-derived 35-kDa protein stimulated a gamma interferon-secreting T-cell proliferative response in the majority of paucibacillary leprosy patients and healthy contacts of leprosy patients tested. Cellular responses to the protein in patients with multibacillary leprosy were weak or absent, consistent with hyporesponsiveness to M. leprae characteristic of this form of the disease. Almost all leprosy patients and contacts recognized the 35-kDa protein by either a T-cell proliferative or an immunoglobulin G antibody response, whereas few tuberculosis patients recognized the antigen. This specificity was confirmed in guinea pigs, with the 35-kDa protein eliciting strong delayed-type hypersensitivity in M. leprae-sensitized animals but not in those sensitized with Mycobacterium tuberculosis or Mycobacterium bovis BCG. Therefore, the M. leprae 35-kDa protein appears to be a major and relatively specific target of the human immune response to M. leprae and is a potential component of a diagnostic test to detect exposure to leprosy or a vaccine to combat the disease.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.