Plasmid RP1-mediated susceptibility of Acinetobacter calcoaceticus to rat polymorphonuclear leukocyte granule contents

M. J. Loeffelholz, M. C. Modrzakowski

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

The resistance plasmid RP1 was transferred by conjugation to a plasmidless strain of Acinetobacter calcoaceticus. Acquisition and expression of RP1 by A. calcoaceticus HO1-N was associated with an increase in sensitivity to the antimicrobial activity of extracted contents from rat polymorphonuclear leukocyte granules. Plasmid RP1-associated antibiotic resistance and sensitivity to granule contents were cured by exposure to acridine orange. Assays with granule extract fractions separated by fast protein liquid chromatography showed myeloperoxidase, protease, and lysozyme fractions to possess little or no antimicrobial activity against the A. calcoaceticus strains. A protein fraction designated peak D, containing two low-molecular-weight cationic peptides, did possess antimicrobial activity against both HO1-N and HO1-N(RP1) strains, with the HO1-N(RP1) strain being significantly more sensitive.

Original languageEnglish (US)
Pages (from-to)705-709
Number of pages5
JournalInfection and Immunity
Volume54
Issue number3
StatePublished - 1986
Externally publishedYes

Fingerprint

Acinetobacter calcoaceticus
Neutrophils
Plasmids
Antimicrobial Cationic Peptides
Acridine Orange
Muramidase
Microbial Drug Resistance
Liquid Chromatography
Peroxidase
Proteins
Peptide Hydrolases
Molecular Weight

ASJC Scopus subject areas

  • Immunology

Cite this

Plasmid RP1-mediated susceptibility of Acinetobacter calcoaceticus to rat polymorphonuclear leukocyte granule contents. / Loeffelholz, M. J.; Modrzakowski, M. C.

In: Infection and Immunity, Vol. 54, No. 3, 1986, p. 705-709.

Research output: Contribution to journalArticle

@article{73b642cb320042f7aa56720b2d197bfc,
title = "Plasmid RP1-mediated susceptibility of Acinetobacter calcoaceticus to rat polymorphonuclear leukocyte granule contents",
abstract = "The resistance plasmid RP1 was transferred by conjugation to a plasmidless strain of Acinetobacter calcoaceticus. Acquisition and expression of RP1 by A. calcoaceticus HO1-N was associated with an increase in sensitivity to the antimicrobial activity of extracted contents from rat polymorphonuclear leukocyte granules. Plasmid RP1-associated antibiotic resistance and sensitivity to granule contents were cured by exposure to acridine orange. Assays with granule extract fractions separated by fast protein liquid chromatography showed myeloperoxidase, protease, and lysozyme fractions to possess little or no antimicrobial activity against the A. calcoaceticus strains. A protein fraction designated peak D, containing two low-molecular-weight cationic peptides, did possess antimicrobial activity against both HO1-N and HO1-N(RP1) strains, with the HO1-N(RP1) strain being significantly more sensitive.",
author = "Loeffelholz, {M. J.} and Modrzakowski, {M. C.}",
year = "1986",
language = "English (US)",
volume = "54",
pages = "705--709",
journal = "Infection and Immunity",
issn = "0019-9567",
publisher = "American Society for Microbiology",
number = "3",

}

TY - JOUR

T1 - Plasmid RP1-mediated susceptibility of Acinetobacter calcoaceticus to rat polymorphonuclear leukocyte granule contents

AU - Loeffelholz, M. J.

AU - Modrzakowski, M. C.

PY - 1986

Y1 - 1986

N2 - The resistance plasmid RP1 was transferred by conjugation to a plasmidless strain of Acinetobacter calcoaceticus. Acquisition and expression of RP1 by A. calcoaceticus HO1-N was associated with an increase in sensitivity to the antimicrobial activity of extracted contents from rat polymorphonuclear leukocyte granules. Plasmid RP1-associated antibiotic resistance and sensitivity to granule contents were cured by exposure to acridine orange. Assays with granule extract fractions separated by fast protein liquid chromatography showed myeloperoxidase, protease, and lysozyme fractions to possess little or no antimicrobial activity against the A. calcoaceticus strains. A protein fraction designated peak D, containing two low-molecular-weight cationic peptides, did possess antimicrobial activity against both HO1-N and HO1-N(RP1) strains, with the HO1-N(RP1) strain being significantly more sensitive.

AB - The resistance plasmid RP1 was transferred by conjugation to a plasmidless strain of Acinetobacter calcoaceticus. Acquisition and expression of RP1 by A. calcoaceticus HO1-N was associated with an increase in sensitivity to the antimicrobial activity of extracted contents from rat polymorphonuclear leukocyte granules. Plasmid RP1-associated antibiotic resistance and sensitivity to granule contents were cured by exposure to acridine orange. Assays with granule extract fractions separated by fast protein liquid chromatography showed myeloperoxidase, protease, and lysozyme fractions to possess little or no antimicrobial activity against the A. calcoaceticus strains. A protein fraction designated peak D, containing two low-molecular-weight cationic peptides, did possess antimicrobial activity against both HO1-N and HO1-N(RP1) strains, with the HO1-N(RP1) strain being significantly more sensitive.

UR - http://www.scopus.com/inward/record.url?scp=0022980177&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022980177&partnerID=8YFLogxK

M3 - Article

C2 - 3781624

AN - SCOPUS:0022980177

VL - 54

SP - 705

EP - 709

JO - Infection and Immunity

JF - Infection and Immunity

SN - 0019-9567

IS - 3

ER -