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Infection and immunity2001; 69(12); 7616-7624; doi: 10.1128/IAI.69.12.7616-7624.2001

Molecular characterization of thermoinduced immunogenic proteins Q1p42 and Hsp15 of Leptospira interrogans.

Abstract: Leptospira interrogans is a mammalian pathogen which must adapt to a range of new environmental conditions including temperature change when it infects new hosts. In vitro studies of organisms cultured at 30 degrees C and shifted to 37 degrees C for 5 to 7 days have confirmed that synthesis of several proteins involved in equine infection is regulated in response to temperature change (J. E. Nally, J. F. Timoney, and B. Stevenson, Infect. Immun. 69:400-404, 2001). In order to specifically identify antigenic proteins upregulated at 37 degrees C, groups of three ponies were immunized with organisms shifted to 37 degrees C for 5 to 7 days or with organisms maintained at 30 degrees C. A lambda ZAP II genomic DNA library was screened with the pool of antisera to organisms shifted to 37 degrees C. Clones reactive with this pool but unreactive with the pool of pony antisera to organisms cultured at 30 degrees C were selected for further analysis. Sequence analysis of the first two clones identified open reading frames for proteins designated Qlp42 and Hsp15. Qlp42 is predicted to be an outer membrane lipoprotein. Its synthesis was upregulated when cultures were shifted from 30 to 37 degrees C and downregulated when cultures were shifted from 37 to 30 degrees C. Although the predicted molecular mass of Qlp42 is 39.8 kDa for the mature protein, Qlp42-specific equine antiserum was reactive with two bands of 30 and 29.5 kDa. Hsp15 is a stress response protein and a member of the Hsp20/alpha-crystallin family. PCR detected homologues of qlp42 and hsp15 in pathogenic serovars of L. interrogans but not in the nonpathogenic Leptospira biflexa. Enzyme-linked immunosorbent assays of antibody in convalescent sera from mares naturally infected with L. interrogans suggest that Qlp42 is expressed during leptospiral infection.
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Publication Date: 2001-11-14 PubMed ID: 11705941PubMed Central: PMC98855DOI: 10.1128/IAI.69.12.7616-7624.2001Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The study focuses on the genetic analysis and characterization of two proteins, Q1p42 and Hsp15, in the pathogen Leptospira interrogans. They found that these two proteins are involved and adapt to temperature changes when the pathogen infects new hosts.

Research Methodology

  • The researchers started off studying the organisms at a controlled 30 degrees Celsius and then adjusted the temperature to 37 degrees for between 5 to 7 days.
  • This study was in an effort to identify the proteins that were being activated at the higher temperature. To do this, they immunized ponies in groups of three, with the organisms that had been heated to 37 degrees Celsius for the said duration, and others with organisms kept at 30 degrees Celsius.
  • To identify the antigenic proteins that were active at the higher temperature of 37 degrees, the researchers used a lambda ZAP II genomic DNA library and screened it with a pool of antisera from organisms that were heated up to 37 degrees Celsius.
  • They selected clones that reacted with this pool for further analysis but did not react with the pony antisera to organisms cultured at 30 degrees Celsius.

Findings

  • The results from the sequence analysis identified two proteins designated as Qlp42 and Hsp15 from the selected clones.
  • Qlp42, which was found to be an outer membrane lipoprotein, showed increased synthesis when temperatures moved from 30 to 37 degrees Celsius, and a decrease was observed when the temperatures were reduced back to 30 degrees Celsius.
  • Another interesting finding was that even if Qlp42 is predicted to be 39.8 kDa for the mature protein, the Qlp42-specific equine antiserum reacted with two bands of 30 and 29.5 kDa.
  • Hsp15 was identified to be a stress response protein and also a member of the Hsp20/alpha-crystallin family.
  • PCR detected homologues of qlp42 and hsp15 in pathogenic serovars of Leptospira interrogans but not in the nonpathogenic Leptospira biflexa.
  • An enzyme-linked immunosorbent assay of antibody in convalescent sera from mares naturally infected with Leptospira interrogans hinted that Qlp42 is likely expressed during leptospiral infection.

Conclusion and Potential Implications

The research concludes that the proteins Q1p42 and Hsp15 are critical in the adaptation of Leptospira interrogans to new environmental conditions when switching hosts. Understanding this adaptive mechanism can help develop effective vaccines to counter infections. It is also suggested that the temperature inducement of these proteins might be a key factor in the pathogenesis of the Leptospira interrogans infection.

Cite This Article

APA
Nally JE, Artiushin S, Timoney JF. (2001). Molecular characterization of thermoinduced immunogenic proteins Q1p42 and Hsp15 of Leptospira interrogans. Infect Immun, 69(12), 7616-7624. https://doi.org/10.1128/IAI.69.12.7616-7624.2001

Publication

Infection and immunity
ISSN: 0019-9567
NlmUniqueID: 0246127
Country: United States
Language: English
Volume: 69
Issue: 12
Pages: 7616-7624

Researcher Affiliations

Nally, J E
  • Department of Veterinary Science, University of Kentucky, Lexington, Kentucky 40546-0099, USA.
Artiushin, S
    Timoney, J F

      MeSH Terms

      • Amino Acid Sequence
      • Animals
      • Antibodies, Bacterial / immunology
      • Antibody Specificity
      • Antigens, Bacterial / genetics
      • Antigens, Bacterial / immunology
      • Bacterial Outer Membrane Proteins / genetics
      • Bacterial Outer Membrane Proteins / immunology
      • Base Sequence
      • Convalescence
      • DNA-Binding Proteins / genetics
      • DNA-Binding Proteins / immunology
      • Escherichia coli Proteins
      • Female
      • Gene Expression Regulation, Bacterial
      • Genomic Library
      • Heat-Shock Proteins / genetics
      • Heat-Shock Proteins / immunology
      • Horse Diseases / blood
      • Horse Diseases / immunology
      • Horses
      • Hot Temperature
      • Leptospira interrogans / genetics
      • Leptospira interrogans / immunology
      • Leptospirosis / blood
      • Leptospirosis / immunology
      • Leptospirosis / veterinary
      • Lipoproteins / genetics
      • Lipoproteins / immunology
      • Molecular Sequence Data
      • Sequence Analysis, DNA
      • Sequence Homology, Amino Acid
      • Up-Regulation

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      This article has been cited 33 times.
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