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Title: Characterization of a major 31-kilodalton peptidoglycan-bound protein of Legionella pneumophila

Abstract

A 31-kilodalton (kDa) protein was solubilized from the peptidoglycan (PG) fraction of Legionella pneumophila after treatment with either N-acetylmuramidase from the fungus Chalaropsis sp. or with mutanolysin from Streptomyces globisporus. The protein exhibited a ladderlike banding pattern by autoradiography when radiolabeled ((35S)cysteine or (35S)methionine) PG material was extensively treated with hen lysozyme. The banding patterns ranging between 31 and 45 kDa and between 55 and 60 kDa resolved as a single 31-kDa protein when the material was subsequently treated with N-acetylmuramidase. Analysis of the purified 31-kDa protein for diaminopimelic acid by gas chromatography revealed 1 mol of diaminopimelic acid per mol of protein. When outer membrane PG material containing the major outer membrane porin protein was treated with N-acetylmuramidase or mutanolysin, both the 28.5-kDa major outer membrane protein and the 31-kDa protein were solubilized from the PG material under reducing conditions. In the absence of 2-mercaptoethanol, a high-molecular-mass complex (100 kDa) was resolved. The results of this study indicate that a 31-kDa PG-bound protein is a major component of the cell wall of L. pneumophila whose function may be to anchor the major outer membrane protein to PG. Finally, a survey of other Legionella species and other serogroups of L.more » pneumophila suggested that PG-bound proteins may be a common feature of this genus.« less

Authors:
;  [1]
  1. Univ. of Tennessee, Memphis (USA)
Publication Date:
OSTI Identifier:
6746885
Resource Type:
Journal Article
Journal Name:
Journal of Bacteriology; (USA)
Additional Journal Information:
Journal Volume: 172:5; Journal ID: ISSN 0021-9193
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; GLYCOPROTEINS; CHEMICAL COMPOSITION; LEGIONELLA PNEUMOPHILA; BIOCHEMISTRY; AUTORADIOGRAPHY; CYSTEINE; ELECTROPHORESIS; GLYCOSYL HYDROLASES; METHIONINE; MOLECULAR WEIGHT; PORINS; SULFUR 35; AMINO ACIDS; BACTERIA; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; CARBOXYLIC ACIDS; CHEMISTRY; DAYS LIVING RADIOISOTOPES; DRUGS; ENZYMES; EVEN-ODD NUCLEI; HYDROLASES; ISOTOPES; LIGHT NUCLEI; LIPOTROPIC FACTORS; MEMBRANE PROTEINS; MICROORGANISMS; NUCLEI; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC SULFUR COMPOUNDS; PROTEINS; RADIOISOTOPES; SULFUR ISOTOPES; THIOLS; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Butler, C A, and Hoffman, P S. Characterization of a major 31-kilodalton peptidoglycan-bound protein of Legionella pneumophila. United States: N. p., 1990. Web.
Butler, C A, & Hoffman, P S. Characterization of a major 31-kilodalton peptidoglycan-bound protein of Legionella pneumophila. United States.
Butler, C A, and Hoffman, P S. 1990. "Characterization of a major 31-kilodalton peptidoglycan-bound protein of Legionella pneumophila". United States.
@article{osti_6746885,
title = {Characterization of a major 31-kilodalton peptidoglycan-bound protein of Legionella pneumophila},
author = {Butler, C A and Hoffman, P S},
abstractNote = {A 31-kilodalton (kDa) protein was solubilized from the peptidoglycan (PG) fraction of Legionella pneumophila after treatment with either N-acetylmuramidase from the fungus Chalaropsis sp. or with mutanolysin from Streptomyces globisporus. The protein exhibited a ladderlike banding pattern by autoradiography when radiolabeled ((35S)cysteine or (35S)methionine) PG material was extensively treated with hen lysozyme. The banding patterns ranging between 31 and 45 kDa and between 55 and 60 kDa resolved as a single 31-kDa protein when the material was subsequently treated with N-acetylmuramidase. Analysis of the purified 31-kDa protein for diaminopimelic acid by gas chromatography revealed 1 mol of diaminopimelic acid per mol of protein. When outer membrane PG material containing the major outer membrane porin protein was treated with N-acetylmuramidase or mutanolysin, both the 28.5-kDa major outer membrane protein and the 31-kDa protein were solubilized from the PG material under reducing conditions. In the absence of 2-mercaptoethanol, a high-molecular-mass complex (100 kDa) was resolved. The results of this study indicate that a 31-kDa PG-bound protein is a major component of the cell wall of L. pneumophila whose function may be to anchor the major outer membrane protein to PG. Finally, a survey of other Legionella species and other serogroups of L. pneumophila suggested that PG-bound proteins may be a common feature of this genus.},
doi = {},
url = {https://www.osti.gov/biblio/6746885}, journal = {Journal of Bacteriology; (USA)},
issn = {0021-9193},
number = ,
volume = 172:5,
place = {United States},
year = {Tue May 01 00:00:00 EDT 1990},
month = {Tue May 01 00:00:00 EDT 1990}
}