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Title: Halogenation and proteolysis of complement component C3 on Salmonella typhimurium during phagocytosis by human neutrophils

Abstract

We examined the fate of C component C3 on the surface of Salmonella typhimurium during ingestion by human neutrophils. Initial experiments showed that C3 fragments and C3-acceptor complexes were the major serum ligands which were surface iodinated by canine myeloperoxidase on serum-incubated rough and smooth isolates of S. typhimurium. In contrast, labeled C3 was not identified when the same organisms were ingested by neutrophils in the presence of 125I-Na, a situation previously shown to iodinate particulate targets via the neutrophil myeloperoxidase-halide-H2O2 system. Pretreatment of neutrophils before phagocytosis with the lipid-soluble protease inhibitor diisopropylfluorophosphate (DFP), but not with other protease inhibitors (p-nitrophenylguanidinobenzoate, leupeptin, pepstatin), substantially blocked proteolysis of 125I-C3 on S. typhimurium strain RG108 during ingestion by neutrophils. Purification of neutrophil phagosomes containing S. typhimurium-bearing 125I-C3 showed that DFP but no other protease inhibitors blocked proteolysis of 125I-C3 within phagosomes. Iodinated C3-acceptor complexes were identified by immunoprecipitation from the detergent-insoluble fraction of phagosomes prepared from DFP-treated cells ingesting S. typhimurium in the presence of 125I-Na. These results show that C3 fragments on the surface of S. typhimurium are the major serum ligands which are halogenated and degraded by proteolysis during phagocytosis by human neutrophils, and suggest that the majority of proteolysismore » on the ingested target occurs within the neutrophil phagosome.« less

Authors:
;
Publication Date:
Research Org.:
National Institute of Allergy and Infectious Diseases, Bethesda, MD (USA)
OSTI Identifier:
5904766
Resource Type:
Journal Article
Journal Name:
J. Immunol.; (United States)
Additional Journal Information:
Journal Volume: 142:9
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; COMPLEMENT; PROTEOLYSIS; NEUTROPHILS; PHAGOCYTOSIS; ADSORPTION; ELECTROPHORESIS; ENZYME INHIBITORS; IMMUNOASSAY; IODINE 125; MAN; METABOLISM; PEPTIDE HYDROLASES; PEROXIDASES; SALMONELLA TYPHIMURIUM; TRACER TECHNIQUES; ANIMALS; BACTERIA; BETA DECAY RADIOISOTOPES; BIOLOGICAL MATERIALS; BLOOD; BLOOD CELLS; BODY FLUIDS; CHEMICAL REACTIONS; DAYS LIVING RADIOISOTOPES; DECOMPOSITION; ELECTRON CAPTURE RADIOISOTOPES; ENZYMES; HYDROLASES; INTERMEDIATE MASS NUCLEI; IODINE ISOTOPES; ISOTOPE APPLICATIONS; ISOTOPES; LEUKOCYTES; MAMMALS; MATERIALS; MICROORGANISMS; NUCLEI; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; OXIDOREDUCTASES; PRIMATES; PROTEINS; RADIOISOTOPES; SALMONELLA; SORPTION; VERTEBRATES; 550501* - Metabolism- Tracer Techniques

Citation Formats

Joiner, K A, and Schweinle, J E. Halogenation and proteolysis of complement component C3 on Salmonella typhimurium during phagocytosis by human neutrophils. United States: N. p., 1989. Web.
Joiner, K A, & Schweinle, J E. Halogenation and proteolysis of complement component C3 on Salmonella typhimurium during phagocytosis by human neutrophils. United States.
Joiner, K A, and Schweinle, J E. 1989. "Halogenation and proteolysis of complement component C3 on Salmonella typhimurium during phagocytosis by human neutrophils". United States.
@article{osti_5904766,
title = {Halogenation and proteolysis of complement component C3 on Salmonella typhimurium during phagocytosis by human neutrophils},
author = {Joiner, K A and Schweinle, J E},
abstractNote = {We examined the fate of C component C3 on the surface of Salmonella typhimurium during ingestion by human neutrophils. Initial experiments showed that C3 fragments and C3-acceptor complexes were the major serum ligands which were surface iodinated by canine myeloperoxidase on serum-incubated rough and smooth isolates of S. typhimurium. In contrast, labeled C3 was not identified when the same organisms were ingested by neutrophils in the presence of 125I-Na, a situation previously shown to iodinate particulate targets via the neutrophil myeloperoxidase-halide-H2O2 system. Pretreatment of neutrophils before phagocytosis with the lipid-soluble protease inhibitor diisopropylfluorophosphate (DFP), but not with other protease inhibitors (p-nitrophenylguanidinobenzoate, leupeptin, pepstatin), substantially blocked proteolysis of 125I-C3 on S. typhimurium strain RG108 during ingestion by neutrophils. Purification of neutrophil phagosomes containing S. typhimurium-bearing 125I-C3 showed that DFP but no other protease inhibitors blocked proteolysis of 125I-C3 within phagosomes. Iodinated C3-acceptor complexes were identified by immunoprecipitation from the detergent-insoluble fraction of phagosomes prepared from DFP-treated cells ingesting S. typhimurium in the presence of 125I-Na. These results show that C3 fragments on the surface of S. typhimurium are the major serum ligands which are halogenated and degraded by proteolysis during phagocytosis by human neutrophils, and suggest that the majority of proteolysis on the ingested target occurs within the neutrophil phagosome.},
doi = {},
url = {https://www.osti.gov/biblio/5904766}, journal = {J. Immunol.; (United States)},
number = ,
volume = 142:9,
place = {United States},
year = {Mon May 01 00:00:00 EDT 1989},
month = {Mon May 01 00:00:00 EDT 1989}
}