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Cloning and characterization of high mobility group box protein 1 (HMGB1) of Wuchereria bancrofti and Brugia malayi

Identifieur interne : 004B62 ( Ncbi/Merge ); précédent : 004B61; suivant : 004B63

Cloning and characterization of high mobility group box protein 1 (HMGB1) of Wuchereria bancrofti and Brugia malayi

Auteurs : Sivasakthivel Thirugnanam ; Gnanasekar Munirathinam ; Anandharaman Veerapathran ; Gajalakshmi Dakshinamoorthy ; Maryada V. Reddy ; Kalyanasundaram Ramaswamy

Source :

RBID : PMC:3480192

Abstract

A human homologue of high mobility group box 1 (HMGB1) protein was cloned and characterized from the human filarial parasites Wuchereria bancrofti and Brugia malayi. Sequence analysis showed that W. bancrofti HMGB1 (WbHMGB1) and B. malayi HMGB1 (BmHMGB1) proteins share 99 % sequence identity. Filarial HMGB1 showed typical architectural sequence characteristics of HMGB family of proteins and consisted of only a single HMG box domain that had significant sequence similarity to the pro-inflammatory B box domain of human HMGB1. When incubated with mouse peritoneal macrophages and human promyelocytic leukemia cells, rBmHMGB1 induced secretion of significant levels of pro-inflammatory cytokines such as TNF-α, GM-CSF, and IL-6. Functional analysis also showed that the filarial HMGB1 proteins can bind to supercoiled DNA similar to other HMG family of proteins. BmHMGB1 protein is expressed in the adult and microfilarial stages of the parasite and is found in the excretory secretions of the live parasites. These findings suggest that filarial HMGB1 may have a significant role in lymphatic pathology associated with lymphatic filariasis.


Url:
DOI: 10.1007/s00436-012-2878-x
PubMed: 22402610
PubMed Central: 3480192

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PMC:3480192

Le document en format XML

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<name sortKey="Thirugnanam, Sivasakthivel" sort="Thirugnanam, Sivasakthivel" uniqKey="Thirugnanam S" first="Sivasakthivel" last="Thirugnanam">Sivasakthivel Thirugnanam</name>
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<name sortKey="Reddy, Maryada V" sort="Reddy, Maryada V" uniqKey="Reddy M" first="Maryada V." last="Reddy">Maryada V. Reddy</name>
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<name sortKey="Ramaswamy, Kalyanasundaram" sort="Ramaswamy, Kalyanasundaram" uniqKey="Ramaswamy K" first="Kalyanasundaram" last="Ramaswamy">Kalyanasundaram Ramaswamy</name>
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<title level="j">Parasitology research</title>
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<p id="P1">A human homologue of high mobility group box 1 (HMGB1) protein was cloned and characterized from the human filarial parasites
<italic>Wuchereria bancrofti</italic>
and
<italic>Brugia malayi</italic>
. Sequence analysis showed that
<italic>W. bancrofti</italic>
HMGB1 (WbHMGB1) and
<italic>B. malayi</italic>
HMGB1 (BmHMGB1) proteins share 99 % sequence identity. Filarial HMGB1 showed typical architectural sequence characteristics of HMGB family of proteins and consisted of only a single HMG box domain that had significant sequence similarity to the pro-inflammatory B box domain of human HMGB1. When incubated with mouse peritoneal macrophages and human promyelocytic leukemia cells, rBmHMGB1 induced secretion of significant levels of pro-inflammatory cytokines such as TNF-α, GM-CSF, and IL-6. Functional analysis also showed that the filarial HMGB1 proteins can bind to supercoiled DNA similar to other HMG family of proteins. BmHMGB1 protein is expressed in the adult and microfilarial stages of the parasite and is found in the excretory secretions of the live parasites. These findings suggest that filarial HMGB1 may have a significant role in lymphatic pathology associated with lymphatic filariasis.</p>
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<journal-id journal-id-type="iso-abbrev">Parasitol. Res.</journal-id>
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<article-title>Cloning and characterization of high mobility group box protein 1 (HMGB1) of
<italic>Wuchereria bancrofti</italic>
and
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<name>
<surname>Thirugnanam</surname>
<given-names>Sivasakthivel</given-names>
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<aff id="A1">Department of Biomedical Sciences, College of Medicine, University of Illinois, Rockford, IL 61107, USA</aff>
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<contrib contrib-type="author">
<name>
<surname>Munirathinam</surname>
<given-names>Gnanasekar</given-names>
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<aff id="A2">Department of Biomedical Sciences, College of Medicine, University of Illinois, Rockford, IL 61107, USA</aff>
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<contrib contrib-type="author">
<name>
<surname>Veerapathran</surname>
<given-names>Anandharaman</given-names>
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<aff id="A3">Department of Biomedical Sciences, College of Medicine, University of Illinois, Rockford, IL 61107, USA</aff>
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<contrib contrib-type="author">
<name>
<surname>Dakshinamoorthy</surname>
<given-names>Gajalakshmi</given-names>
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<aff id="A4">Department of Biomedical Sciences, College of Medicine, University of Illinois, Rockford, IL 61107, USA</aff>
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<contrib contrib-type="author">
<name>
<surname>Reddy</surname>
<given-names>Maryada V.</given-names>
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<aff id="A5">Department of Biochemistry, Mahatma Gandhi Institute of Medical Sciences, Wardha, India</aff>
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<contrib contrib-type="author">
<name>
<surname>Ramaswamy</surname>
<given-names>Kalyanasundaram</given-names>
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<email>ramswamy@uic.edu</email>
<aff id="A6">Department of Biomedical Sciences, College of Medicine, University of Illinois, Rockford, IL 61107, USA</aff>
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<author-notes>
<fn id="FN1" fn-type="equal">
<p>Sivasakthivel Thirugnanam and Gnanasekar Munirathinam contributed equally to the study.</p>
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<pub-date pub-type="nihms-submitted">
<day>26</day>
<month>9</month>
<year>2012</year>
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<pub-date pub-type="epub">
<day>09</day>
<month>3</month>
<year>2012</year>
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<pub-date pub-type="pmc-release">
<day>24</day>
<month>10</month>
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<volume>111</volume>
<issue>2</issue>
<fpage>619</fpage>
<lpage>627</lpage>
<permissions>
<copyright-statement>© Springer-Verlag 2012</copyright-statement>
<copyright-year>2012</copyright-year>
</permissions>
<abstract>
<p id="P1">A human homologue of high mobility group box 1 (HMGB1) protein was cloned and characterized from the human filarial parasites
<italic>Wuchereria bancrofti</italic>
and
<italic>Brugia malayi</italic>
. Sequence analysis showed that
<italic>W. bancrofti</italic>
HMGB1 (WbHMGB1) and
<italic>B. malayi</italic>
HMGB1 (BmHMGB1) proteins share 99 % sequence identity. Filarial HMGB1 showed typical architectural sequence characteristics of HMGB family of proteins and consisted of only a single HMG box domain that had significant sequence similarity to the pro-inflammatory B box domain of human HMGB1. When incubated with mouse peritoneal macrophages and human promyelocytic leukemia cells, rBmHMGB1 induced secretion of significant levels of pro-inflammatory cytokines such as TNF-α, GM-CSF, and IL-6. Functional analysis also showed that the filarial HMGB1 proteins can bind to supercoiled DNA similar to other HMG family of proteins. BmHMGB1 protein is expressed in the adult and microfilarial stages of the parasite and is found in the excretory secretions of the live parasites. These findings suggest that filarial HMGB1 may have a significant role in lymphatic pathology associated with lymphatic filariasis.</p>
</abstract>
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<funding-source country="United States">National Institute of Allergy and Infectious Diseases Extramural Activities : NIAID</funding-source>
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<name sortKey="Veerapathran, Anandharaman" sort="Veerapathran, Anandharaman" uniqKey="Veerapathran A" first="Anandharaman" last="Veerapathran">Anandharaman Veerapathran</name>
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