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Home / Equine Research Bank / Infect Immun / Selective inhibition of microbial serine proteases by eNAP-2...
Infection and immunity1993; 61(7); 2991-2994; doi: 10.1128/iai.61.7.2991-2994.1993

Selective inhibition of microbial serine proteases by eNAP-2, an antimicrobial peptide from equine neutrophils.

Abstract: Equine neutrophil antimicrobial peptide 2 (eNAP-2), a recently described antimicrobial peptide isolated from equine neutrophils, was found to selectively inactivate microbial serine proteases (subtilisin A and proteinase K) without inhibiting mammalian serine proteases (human neutrophil elastase, human cathepsin G, and bovine pancreatic trypsin). Although the primary structure of eNAP-2 resembled that of several known antiproteases that belong to the 4-disulfide core peptide family, this pattern of selectivity is unique. eNAP-2 formed a noncovalent complex with native subtilisin A or proteinase K but did not associate with these enzymes if they had been treated with phenylmethylsulfonyl fluoride, a serine protease inhibitor. The eNAP-2-microbial protease complex was disrupted by boiling or by exposure to low pH. We suggest that eNAP-2 exerted selective antiproteinase activity by binding tightly but noncovalently to the active site of subtilisin A or proteinase K. Since microbial exoproteases may act as virulence factors, the combined antimicrobial and antiprotease activities of eNAP-2 could allow it to play an important role in neutrophil-mediated antimicrobial defenses.
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Publication Date: 1993-07-01 PubMed ID: 8514405PubMed Central: PMC280950DOI: 10.1128/iai.61.7.2991-2994.1993Google Scholar: Lookup
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  • Journal Article
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  • Non-U.S. Gov't
  • Research Support
  • U.S. Gov't
  • P.H.S.

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 research article discusses the role of eNAP-2, a type of antimicrobial peptide derived from equine neutrophils, in selectively disabling the activity of microbial serine proteases, potentially aiding in the body’s antimicrobial defense system.

Overview of the Research

  • The study focuses on the action of equine neutrophil antimicrobial peptide 2 (eNAP-2), which is an antimicrobial peptide isolated from equine neutrophils, a type of white blood cell in horses.
  • This peptide has been observed to selectively inhibit microbial serine proteases like subtilisin A and proteinase K. Interestingly, it does not impact mammalian serine proteases such as human neutrophil elastase, cathepsin G, and bovine pancreatic trypsin.

Unique Selectivity and Mechanism of Action of eNAP-2

  • When looking at its primary structure, it was found that eNAP-2 bears similarities with known antiproteases belonging to the 4-disulfide core peptide family, but its ability to selectively inhibit microbial proteases is rather unique.
  • Researchers discovered that eNAP-2 forms a noncovalent complex with native subtilisin A or proteinase K. However, this association is not formed if these enzymes are treated with phenylmethylsulfonyl fluoride, which is a serine protease inhibitor.
  • This eNAP-2-microbial protease complex can be disrupted by boiling or exposure to low pH conditions.
  • The researchers concluded that eNAP-2 exerts selective antiproteinase activity by binding tightly, albeit noncovalently, to the active site of either subtilisin A or proteinase K.

Potential Role of eNAP-2 in Antimicrobial Defenses

  • Microbial exoproteases are often seen as plant and animal pathogens and can act as virulence factors, helping microbes to invade host cells, evade the immune system, or acquire nutrients.
  • The unique antimicrobial and antiprotease activities of eNAP-2 gives it the potential to play a significant role in the antimicrobial defenses of the body, specifically those mediated by neutrophils.
  • By effectively binding to and disabling these microbial serine proteases, eNAP-2 could limit the virulence of certain microbes, enhancing the immune response.

Cite This Article

APA
Couto MA, Harwig SS, Lehrer RI. (1993). Selective inhibition of microbial serine proteases by eNAP-2, an antimicrobial peptide from equine neutrophils. Infect Immun, 61(7), 2991-2994. https://doi.org/10.1128/iai.61.7.2991-2994.1993

Publication

Infection and immunity
ISSN: 0019-9567
NlmUniqueID: 0246127
Country: United States
Language: English
Volume: 61
Issue: 7
Pages: 2991-2994

Researcher Affiliations

Couto, M A
  • Department of Medicine, UCLA School of Medicine 90024.
Harwig, S S
    Lehrer, R I

      MeSH Terms

      • Animals
      • Anti-Infective Agents / pharmacology
      • Blood Proteins / pharmacology
      • Endopeptidase K
      • Horses
      • Neutrophils / chemistry
      • Serine Endopeptidases / metabolism
      • Serine Proteinase Inhibitors / pharmacology
      • Subtilisins / antagonists & inhibitors

      Grant Funding

      • AI22839 / NIAID NIH HHS
      • AI29595 / NIAID NIH HHS

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      Citations

      This article has been cited 15 times.
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