The vsp Locus of Mycoplasma bovis: Gene Organization and Structural Features

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Published inJournal of Bacteriology Vol. 181; no. 18; pp. 5734 - 5741
Main Authors Lysnyansky, Inessa, Sachse, Konrad, Rosenbusch, Ricardo, Levisohn, Sharon, Yogev, David
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.09.1999
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Abstract Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JB .asm.org, visit: JB       
AbstractList Major lipoprotein antigens, known as variable membrane surface lipoproteins (Vsps), on the surface of the bovine pathogen Mycoplasma bovis were shown to spontaneously undergo noncoordinate phase variation between ON and OFF expression states. The high rate of Vsp phenotypic switching was also shown to be linked with DNA rearrangements that occur at high frequency in the M. bovis chromosome (I. Lysnyansky, R. Rosengarten, and D. Yogev, J. Bacteriol. 178:5395–5401, 1996). In the present study, 13 single-copy vsp genes organized in a chromosomal cluster were identified and characterized. All vsp genes encode highly conserved N-terminal domains for membrane insertion and lipoprotein processing but divergent mature Vsp proteins. About 80% of each vsp coding region is composed of reiterated coding sequences that create a periodic polypeptide structure. Eighteen distinct repetitive domains of different lengths and amino acid sequences are distributed within the products of the various vsp genes that are subject to size variation due to spontaneous insertions or deletions of these periodic units. Some of these repeats were found to be present in only one Vsp family member, whereas other repeats recurred at variable locations in several Vsps. Each vsp gene is also 5′ linked to a highly homologous upstream region composed of two internal cassettes. The findings that rearrangement events are associated with Vsp phenotypic switching and that multiple regions of high sequence similarity are present upstream of the vsp genes and within the vsp coding regions suggest that modulation of the Vsp antigenic repertoire is determined by recombination processes that occur at a high frequency within the vsp locus of M. bovis .
Major lipoprotein antigens, known as variable membrane surface lipoproteins (Vsps), on the surface of the bovine pathogen Mycoplasma bovis were shown to spontaneously undergo noncoordinate phase variation between ON and OFF expression states. The high rate of Vsp phenotypic switching was also shown to be linked with DNA rearrangements that occur at high frequency in the M. bovis chromosome (I. Lysnyansky, R. Rosengarten, and D. Yogev, J. Bacteriol. 178:5395-5401, 1996). In the present study, 13 single-copy vsp genes organized in a chromosomal cluster were identified and characterized. All vsp genes encode highly conserved N-terminal domains for membrane insertion and lipoprotein processing but divergent mature Vsp proteins. About 80% of each vsp coding region is composed of reiterated coding sequences that create a periodic polypeptide structure. Eighteen distinct repetitive domains of different lengths and amino acid sequences are distributed within the products of the various vsp genes that are subject to size variation due to spontaneous insertions or deletions of these periodic units. Some of these repeats were found to be present in only one Vsp family member, whereas other repeats recurred at variable locations in several Vsps. Each vsp gene is also 5' linked to a highly homologous upstream region composed of two internal cassettes. The findings that rearrangement events are associated with Vsp phenotypic switching and that multiple regions of high sequence similarity are present upstream of the vsp genes and within the vsp coding regions suggest that modulation of the Vsp antigenic repertoire is determined by recombination processes that occur at a high frequency within the vsp locus of M. bovis.
Major lipoprotein antigens, known as variable membrane surface lipoproteins (Vsps), on the surface of the bovine pathogen Mycoplasma bovis were shown to spontaneously undergo noncoordinate phase variation between ON and OFF expression states. The high rate of Vsp phenotypic switching was also shown to be linked with DNA rearrangements that occur at high frequency in the M. bovis chromosome (I. Lysnyansky, R. Rosengarten, and D. Yogev, J. Bacteriol. 178:5395-5401, 1996). In the present study, 13 single-copy vsp genes organized in a chromosomal cluster were identified and characterized. All vsp genes encode highly conserved N-terminal domains for membrane insertion and lipoprotein processing but divergent mature Vsp proteins. About 80% of each vsp coding region is composed of reiterated coding sequences that create a periodic polypeptide structure. Eighteen distinct repetitive domains of different lengths and amino acid sequences are distributed within the products of the various vsp genes that are subject to size variation due to spontaneous insertions or deletions of these periodic units. Some of these repeats were found to be present in only one Vsp family member, whereas other repeats recurred at variable locations in several Vsps. Each vsp gene is also 5' linked to a highly homologous upstream region composed of two internal cassettes. The findings that rearrangement events are associated with Vsp phenotypic switching and that multiple regions of high sequence similarity are present upstream of the vsp genes and within the vsp coding regions suggest that modulation of the Vsp antigenic repertoire is determined by recombination processes that occur at a high frequency within the vsp locus of M. bovis.Major lipoprotein antigens, known as variable membrane surface lipoproteins (Vsps), on the surface of the bovine pathogen Mycoplasma bovis were shown to spontaneously undergo noncoordinate phase variation between ON and OFF expression states. The high rate of Vsp phenotypic switching was also shown to be linked with DNA rearrangements that occur at high frequency in the M. bovis chromosome (I. Lysnyansky, R. Rosengarten, and D. Yogev, J. Bacteriol. 178:5395-5401, 1996). In the present study, 13 single-copy vsp genes organized in a chromosomal cluster were identified and characterized. All vsp genes encode highly conserved N-terminal domains for membrane insertion and lipoprotein processing but divergent mature Vsp proteins. About 80% of each vsp coding region is composed of reiterated coding sequences that create a periodic polypeptide structure. Eighteen distinct repetitive domains of different lengths and amino acid sequences are distributed within the products of the various vsp genes that are subject to size variation due to spontaneous insertions or deletions of these periodic units. Some of these repeats were found to be present in only one Vsp family member, whereas other repeats recurred at variable locations in several Vsps. Each vsp gene is also 5' linked to a highly homologous upstream region composed of two internal cassettes. The findings that rearrangement events are associated with Vsp phenotypic switching and that multiple regions of high sequence similarity are present upstream of the vsp genes and within the vsp coding regions suggest that modulation of the Vsp antigenic repertoire is determined by recombination processes that occur at a high frequency within the vsp locus of M. bovis.
Major lipoprotein antigens, known as variable membrane surface lipoproteins (Vsps), on the surface of the bovine pathogen Mycoplasma bovis were shown to spontaneously undergo noncoordinate phase variation between ON and OFF expression states.
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Author David Yogev
Inessa Lysnyansky
Sharon Levisohn
Ricardo Rosenbusch
Konrad Sachse
AuthorAffiliation Department of Membrane and Ultrastructure Research, The Hebrew University—Hadassah Medical School, Jerusalem 91120, 1 and Mycoplasma Unit, Kimron Veterinary Institute, Bet Dagan 50250, 4 Israel; Federal Institute for Health Protection of Consumers and Veterinary Medicine, Division 4, Jena, Germany 2 ; and Veterinary Medical Research Institute, Iowa State University, Ames, Iowa 50011 3
AuthorAffiliation_xml – name: Department of Membrane and Ultrastructure Research, The Hebrew University—Hadassah Medical School, Jerusalem 91120, 1 and Mycoplasma Unit, Kimron Veterinary Institute, Bet Dagan 50250, 4 Israel; Federal Institute for Health Protection of Consumers and Veterinary Medicine, Division 4, Jena, Germany 2 ; and Veterinary Medical Research Institute, Iowa State University, Ames, Iowa 50011 3
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  givenname: Inessa
  surname: Lysnyansky
  fullname: Lysnyansky, Inessa
  organization: <!--label omitted: 1-->Department of Membrane and Ultrastructure Research, The Hebrew University—Hadassah Medical School, Jerusalem 91120,1 and
– sequence: 2
  givenname: Konrad
  surname: Sachse
  fullname: Sachse, Konrad
  organization: <!--label omitted: 2-->Federal Institute for Health Protection of Consumers and Veterinary Medicine, Division 4, Jena, Germany2; and
– sequence: 3
  givenname: Ricardo
  surname: Rosenbusch
  fullname: Rosenbusch, Ricardo
  organization: <!--label omitted: 3-->Veterinary Medical Research Institute, Iowa State University, Ames, Iowa 500113
– sequence: 4
  givenname: Sharon
  surname: Levisohn
  fullname: Levisohn, Sharon
  organization: <!--label omitted: 4-->Mycoplasma Unit, Kimron Veterinary Institute, Bet Dagan 50250,4 Israel
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  fullname: Yogev, David
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/10482515$$D View this record in MEDLINE/PubMed
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Corresponding author. Mailing address: Department of Membrane and Ultrastructure Research, The Hebrew University—Hadassah Medical School, P.O. Box 12272, Jerusalem 91120, Israel. Phone: 972-2-6758-176. Fax: 972-2-6784-010. E-mail: yogev@cc.huji.ac.il.
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Major lipoprotein antigens, known as variable membrane surface lipoproteins (Vsps), on the surface of the bovine pathogen Mycoplasma bovis were shown to...
Major lipoprotein antigens, known as variable membrane surface lipoproteins (Vsps), on the surface of the bovine pathogen Mycoplasma bovis were shown to...
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StartPage 5734
SubjectTerms 5' Untranslated Regions
5' Untranslated Regions - genetics
Amino Acid Sequence
amino acid sequences
Animals
Antigens, Bacterial
bacterial antigens
bacterial proteins
Bacterial Proteins - genetics
Bacteriology
Base Sequence
Cattle
Cell Surfaces
Chromosomes, Bacterial
Cloning, Molecular
Deoxyribonucleic acid
DNA
DNA Probes
genes
Genes, Bacterial
Genetics
lipoproteins
Lipoproteins - genetics
loci
Membrane Proteins
Membrane Proteins - genetics
Molecular Sequence Data
Mycoplasma
Mycoplasma - genetics
Mycoplasma bovis
nucleotide sequences
Open Reading Frames
phenotypic switching
Proteins
Restriction Mapping
Sequence Alignment
Sequence Homology, Nucleic Acid
variable membrane surface lipoproteins
vsp gene
Title The vsp Locus of Mycoplasma bovis: Gene Organization and Structural Features
URI http://jb.asm.org/content/181/18/5734.abstract
https://www.ncbi.nlm.nih.gov/pubmed/10482515
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https://www.proquest.com/docview/49105582
https://www.proquest.com/docview/70034804
https://pubmed.ncbi.nlm.nih.gov/PMC94094
Volume 181
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