Cited by 253Parasites and Host InteractionsCell Adhesion Molecules ResearchHelminth infection and control

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A hookworm glycoprotein that inhibits neutrophil function is a ligand of the integrin CD11b/CD18

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Moyle, M., Foster, D.L., McGrath, D.E., Brown, S.M., Laroche, Y., De Meutter, J., Stanssens, P., Bogowitz, C.A., Fried, V.A., Ely, J.A.·1994·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(17)36982-x

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Abstract

The chronic survival of many endoparasites is dependent on the ability of these organisms to escape the host immune response. Identification of the molecular mechanisms by which these organisms evade this response may yield novel approaches in the development of anti-inflammatory agents. We describe here the discovery and characterization of a novel 41-kilodalton glycoprotein from the canine hookwork (Ancylostoma caninum) that potently inhibits CD11/CD18-dependent neutrophil function in vitro. Neutrophil inhibitory factor (NIF) blocks the adhesion of activated human neutrophils to vascular endothelial cells as well as the release of H2O2 from activated neutrophils, over a similar concentration range (IC50 10-20 nM). Studies aimed at determining the nature of the NIF binding site on neutrophils revealed selective, high affinity binding of this protein to the integrin CD11b/CD18. A cDNA encoding NIF was isolated from a canine hookworm cDNA library. NIF comprises a mature polypeptide of 257 amino acids, preceded by a 17-amino acid leader. The mature protein has 10 cysteines and has seven potential N-linked glycosylation sites. NIF has no significant sequence homologies to any previously reported protein. As such, NIF represents a prototype of a novel class of leukocyte function inhibitors.

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Authors: Moyle, M., Foster, D. L., McGrath, D. E., Brown, S. M., Laroche, Y., De Meutter, J., Stanssens, P., Bogowitz, C. A., Fried, V. A., & Ely, J. A.
Affiliations: New York Medical College (US)
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1994-04
Volume: 269
Issue: 13
Pages: 10008-10015
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(17)36982-x
OpenAlex: W1598106324
Cited by: 253
References: 38
Citations by year: 2026: 2 · 2025: 1 · 2024: 1 · 2023: 5 · 2022: 5 · 2021: 6 · 2020: 7 · 2019: 3 · 2018: 15 · 2017: 3 · 2016: 10 · 2015: 4 · 2014: 11 · 2013: 6 · 2012: 17
FWCI: 9.68
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 9709 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Life Sciences › Immunology and Microbiology › Parasitology › Parasites and Host Interactions
Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
Life Sciences › Immunology and Microbiology › Parasitology › Helminth infection and control
Keywords: hookworm, Ancylostoma caninum, CD11b/CD18 integrin, neutrophil adhesion, parasite immune evasion, glycoproteins, cDNA cloning, cysteine-rich proteins, N-glycosylation, hydrogen peroxide release, anti-inflammatory agents
MeSH terms: Amino Acid Sequence, Ancylostomatoidea, Animals, Base Sequence, Cloning, Molecular, Dogs, Glycoproteins, Humans, Leukocytes, Membrane Proteins, Molecular Sequence Data, Neutrophils, Peptide Fragments, Recombinant Proteins, Protein Biosynthesis, Antigens, CD, Helminth Proteins, Polymerase Chain Reaction, Macrophage-1 Antigen, DNA Primers, DNA, Complementary, CD18 Antigens

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A hookworm glycoprotein that inhibits neutrophil function is a ligand of the integrin CD11b/CD18

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