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Home/Equine Research Bank/Infect Immun/Antibacterial activity of antileukoprotease.
Infection and immunity1996; 64(11); 4520-4524; doi: 10.1128/iai.64.11.4520-4524.1996

Antibacterial activity of antileukoprotease.

Abstract: Antileukoprotease (ALP), or secretory leukocyte proteinase inhibitor, is an endogenous inhibitor of serine proteinases that is present in various external secretions. ALP, one of the major inhibitors of serine proteinases present in the human lung, is a potent reversible inhibitor of elastase and, to a lesser extent, of cathepsin G. In equine neutrophils, an antimicrobial polypeptide that has some of the characteristics of ALP has been identified (M. A. Couto, S. S. L. Harwig, J. S. Cullor, J. P. Hughes, and R. I. Lehrer, Infect. Immun. 60:5042-5047, 1992). This report, together with the cationic nature of ALP, led us to investigate the antimicrobial activity of ALP. ALP was shown to display marked in vitro antibacterial activity against Escherichia coli and Staphylococcus aureus. On a molar basis, the activity of ALP was lower than that of two other cationic antimicrobial polypeptides, lysozyme and defensin. ALP comprises two homologous domains: its proteinase-inhibitory activities are known to be located in the second COOH-terminal domain, and the function of its first NH2-terminal domain is largely unknown. Incubation of intact ALP or its isolated first domain with E. coli or S. aureus resulted in killing of these bacteria, whereas its second domain displayed very little antibacterial activity. Together these data suggest a putative antimicrobial role for the first domain of ALP and indicate that its antimicrobial activity may equip ALP to contribute to host defense against infection.
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Publication Date: 1996-11-01 PubMed ID: 8890201PubMed Central: PMC174407DOI: 10.1128/iai.64.11.4520-4524.1996Google Scholar: Lookup
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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.

This research investigates the antibacterial activity of Antileukoprotease (ALP), a protein found in the human lung, against two types of bacteria, Escherichia coli and Staphylococcus aureus. It suggests that one particular section of the ALP molecule may be responsible for this antimicrobial action and could contribute to the body’s defense against infection.

Introduction to Antileukoprotease (ALP)

  • Antileukoprotease (ALP), also known as secretory leukocyte proteinase inhibitor, is a naturally occurring inhibitor of serine proteinases.
  • It is found in various secretions and is a major inhibitor of serine proteinases in the human lung.
  • The ALP molecule is known to be a potent reversible inhibitor of an enzyme called elastase and less strongly of another enzyme known as cathepsin G.

ALP and Its Antimicrobial Property

  • fPrevious research identified an antimicrobial polypeptide in horse neutrophils with similarities to ALP.
  • Due to this and the ALP molecule’s cationic nature, which means it carries a positive charge, researchers speculated that ALP may have antimicrobial activity.
  • The studies confirmed that ALP indeed has significant in vitro antibacterial activity against Escherichia coli and Staphylococcus aureus, two common types of bacteria.
  • However, when its antibacterial activity was compared on a molar basis, it was found to be less than that of two other positively charged antimicrobial polypeptides, lysozyme and defensin.

Identification of Antimicrobial Role of ALP’s First Domain

  • The ALP molecule is comprised of two homologous domains. The proteinase-inhibitory activities of ALP are located in its second domain, while the function of the first domain was not well-established.
  • Experiments were conducted on both the first and second domain of the ALP molecule. These experiments showed that exposure of either intact ALP or its isolated first domain resulted in the elimination of the bacteria.
  • The second domain of the ALP molecule, on the other hand, showed little to no antibacterial activity.
  • These results suggest that the first domain of the ALP molecule might play an antimicrobial role, enhancing the body’s defence against infection.

Cite This Article

APA
Hiemstra PS, Maassen RJ, Stolk J, Heinzel-Wieland R, Steffens GJ, Dijkman JH. (1996). Antibacterial activity of antileukoprotease. Infect Immun, 64(11), 4520-4524. https://doi.org/10.1128/iai.64.11.4520-4524.1996

Publication

Infection and immunity
ISSN: 0019-9567
NlmUniqueID: 0246127
Country: United States
Language: English
Volume: 64
Issue: 11
Pages: 4520-4524

Researcher Affiliations

Hiemstra, P S
  • Department of Pulmonology, Leiden University Hospital, The Netherlands.
Maassen, R J
    Stolk, J
      Heinzel-Wieland, R
        Steffens, G J
          Dijkman, J H

            MeSH Terms

            • Anti-Bacterial Agents / chemistry
            • Anti-Bacterial Agents / pharmacology
            • Blood Proteins / pharmacology
            • Colony Count, Microbial
            • Defensins
            • Electrophoresis, Polyacrylamide Gel
            • Escherichia coli / drug effects
            • Escherichia coli / growth & development
            • Humans
            • Hydrogen-Ion Concentration
            • Microbial Sensitivity Tests
            • Muramidase / pharmacology
            • Pancreatic Elastase / antagonists & inhibitors
            • Proteinase Inhibitory Proteins, Secretory
            • Proteins / chemistry
            • Proteins / pharmacology
            • Recombinant Proteins / pharmacology
            • Serine Proteinase Inhibitors / pharmacology
            • Staphylococcus aureus / drug effects
            • Staphylococcus aureus / growth & development

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