The SARS Coronavirus 3a protein binds calcium in its cytoplasmic domain.
Identifieur interne : 000F47 ( PubMed/Corpus ); précédent : 000F46; suivant : 000F48The SARS Coronavirus 3a protein binds calcium in its cytoplasmic domain.
Auteurs : Rinki Minakshi ; Kartika Padhan ; Safikur Rehman ; Md Imtaiyaz Hassan ; Faizan AhmadSource :
- Virus research [ 1872-7492 ] ; 2014.
English descriptors
- KwdEn :
- Amino Acid Sequence, Calcium (metabolism), Cytoplasm (virology), Humans, Molecular Sequence Data, Protein Conformation, Protein Structure, Tertiary, SARS Virus (chemistry), SARS Virus (genetics), SARS Virus (metabolism), Severe Acute Respiratory Syndrome (virology), Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (metabolism).
- MESH :
- chemical , chemistry : Viral Proteins.
- chemical , genetics : Viral Proteins.
- chemical , metabolism : Calcium, Viral Proteins.
- chemistry : SARS Virus.
- genetics : SARS Virus.
- metabolism : SARS Virus.
- virology : Cytoplasm, Severe Acute Respiratory Syndrome.
- Amino Acid Sequence, Humans, Molecular Sequence Data, Protein Conformation, Protein Structure, Tertiary.
Abstract
The Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) is a positive stranded RNA virus with ∼30kb genome. Among all open reading frames (orfs) of this virus, the orf3a is the largest, and encodes a protein of 274 amino acids, named as 3a protein. Sequence analysis suggests that the orf3a aligned to one calcium pump present in Plasmodium falciparum and the enzyme glutamine synthetase found in Leptospira interrogans. This sequence similarity was found to be limited only to amino acid residues 209-264 which form the cytoplasmic domain of the orf3a. Furthermore, this region was predicted to be involved in the calcium binding. Owing to this hypothesis, we were driven to establish its calcium binding property in vitro. Here, we expressed and purified the cytoplasmic domain of the 3a protein, called Cyto3a, as a recombinant His-tagged protein in the E. coli. The calcium binding nature was established by performing various staining methods such as ruthenium red and stains-all. (45)Ca overlay method was also done to further support the data. Since the 3a protein forms ion channels, we were interested to see any conformational changes occurring in the Cyot3a upon calcium binding, using fluorescence spectroscopy and circular dichroism. These studies clearly indicate a significant change in the conformation of the Cyto3a protein after binding with calcium. Our results strongly suggest that the cytoplasmic domain of the 3a protein of SARS-CoV binds calcium in vitro, causing a change in protein conformation.
DOI: 10.1016/j.virusres.2014.08.001
PubMed: 25116391
Links to Exploration step
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Electronic address: rinki.minakshi@hotmail.com.</nlm:affiliation></affiliation></author><author><name sortKey="Padhan, Kartika" sort="Padhan, Kartika" uniqKey="Padhan K" first="Kartika" last="Padhan">Kartika Padhan</name><affiliation><nlm:affiliation>International Centre for Genetic Engineering and Biotechnology, New Delhi, India.</nlm:affiliation></affiliation></author><author><name sortKey="Rehman, Safikur" sort="Rehman, Safikur" uniqKey="Rehman S" first="Safikur" last="Rehman">Safikur Rehman</name><affiliation><nlm:affiliation>Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.</nlm:affiliation></affiliation></author><author><name sortKey="Hassan, Md Imtaiyaz" sort="Hassan, Md Imtaiyaz" uniqKey="Hassan M" first="Md Imtaiyaz" last="Hassan">Md Imtaiyaz Hassan</name><affiliation><nlm:affiliation>Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.</nlm:affiliation></affiliation></author><author><name sortKey="Ahmad, Faizan" sort="Ahmad, Faizan" uniqKey="Ahmad F" first="Faizan" last="Ahmad">Faizan Ahmad</name><affiliation><nlm:affiliation>Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:25116391</idno><idno type="pmid">25116391</idno><idno type="doi">10.1016/j.virusres.2014.08.001</idno><idno type="wicri:Area/PubMed/Corpus">000F47</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000F47</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The SARS Coronavirus 3a protein binds calcium in its cytoplasmic domain.</title><author><name sortKey="Minakshi, Rinki" sort="Minakshi, Rinki" uniqKey="Minakshi R" first="Rinki" last="Minakshi">Rinki Minakshi</name><affiliation><nlm:affiliation>International Centre for Genetic Engineering and Biotechnology, New Delhi, India; Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India. Electronic address: rinki.minakshi@hotmail.com.</nlm:affiliation></affiliation></author><author><name sortKey="Padhan, Kartika" sort="Padhan, Kartika" uniqKey="Padhan K" first="Kartika" last="Padhan">Kartika Padhan</name><affiliation><nlm:affiliation>International Centre for Genetic Engineering and Biotechnology, New Delhi, India.</nlm:affiliation></affiliation></author><author><name sortKey="Rehman, Safikur" sort="Rehman, Safikur" uniqKey="Rehman S" first="Safikur" last="Rehman">Safikur Rehman</name><affiliation><nlm:affiliation>Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.</nlm:affiliation></affiliation></author><author><name sortKey="Hassan, Md Imtaiyaz" sort="Hassan, Md Imtaiyaz" uniqKey="Hassan M" first="Md Imtaiyaz" last="Hassan">Md Imtaiyaz Hassan</name><affiliation><nlm:affiliation>Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.</nlm:affiliation></affiliation></author><author><name sortKey="Ahmad, Faizan" sort="Ahmad, Faizan" uniqKey="Ahmad F" first="Faizan" last="Ahmad">Faizan Ahmad</name><affiliation><nlm:affiliation>Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Virus research</title><idno type="eISSN">1872-7492</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Calcium (metabolism)</term><term>Cytoplasm (virology)</term><term>Humans</term><term>Molecular Sequence Data</term><term>Protein Conformation</term><term>Protein Structure, Tertiary</term><term>SARS Virus (chemistry)</term><term>SARS Virus (genetics)</term><term>SARS Virus (metabolism)</term><term>Severe Acute Respiratory Syndrome (virology)</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (genetics)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcium</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Cytoplasm</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Humans</term><term>Molecular Sequence Data</term><term>Protein Conformation</term><term>Protein Structure, Tertiary</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) is a positive stranded RNA virus with ∼30kb genome. Among all open reading frames (orfs) of this virus, the orf3a is the largest, and encodes a protein of 274 amino acids, named as 3a protein. Sequence analysis suggests that the orf3a aligned to one calcium pump present in Plasmodium falciparum and the enzyme glutamine synthetase found in Leptospira interrogans. This sequence similarity was found to be limited only to amino acid residues 209-264 which form the cytoplasmic domain of the orf3a. Furthermore, this region was predicted to be involved in the calcium binding. Owing to this hypothesis, we were driven to establish its calcium binding property in vitro. Here, we expressed and purified the cytoplasmic domain of the 3a protein, called Cyto3a, as a recombinant His-tagged protein in the E. coli. The calcium binding nature was established by performing various staining methods such as ruthenium red and stains-all. (45)Ca overlay method was also done to further support the data. Since the 3a protein forms ion channels, we were interested to see any conformational changes occurring in the Cyot3a upon calcium binding, using fluorescence spectroscopy and circular dichroism. These studies clearly indicate a significant change in the conformation of the Cyto3a protein after binding with calcium. Our results strongly suggest that the cytoplasmic domain of the 3a protein of SARS-CoV binds calcium in vitro, causing a change in protein conformation. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25116391</PMID><DateCompleted><Year>2015</Year><Month>06</Month><Day>04</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1872-7492</ISSN><JournalIssue CitedMedium="Internet"><Volume>191</Volume><PubDate><Year>2014</Year><Month>Oct</Month><Day>13</Day></PubDate></JournalIssue><Title>Virus research</Title><ISOAbbreviation>Virus Res.</ISOAbbreviation></Journal><ArticleTitle>The SARS Coronavirus 3a protein binds calcium in its cytoplasmic domain.</ArticleTitle><Pagination><MedlinePgn>180-3</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.virusres.2014.08.001</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0168-1702(14)00329-3</ELocationID><Abstract><AbstractText>The Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) is a positive stranded RNA virus with ∼30kb genome. Among all open reading frames (orfs) of this virus, the orf3a is the largest, and encodes a protein of 274 amino acids, named as 3a protein. Sequence analysis suggests that the orf3a aligned to one calcium pump present in Plasmodium falciparum and the enzyme glutamine synthetase found in Leptospira interrogans. This sequence similarity was found to be limited only to amino acid residues 209-264 which form the cytoplasmic domain of the orf3a. Furthermore, this region was predicted to be involved in the calcium binding. Owing to this hypothesis, we were driven to establish its calcium binding property in vitro. Here, we expressed and purified the cytoplasmic domain of the 3a protein, called Cyto3a, as a recombinant His-tagged protein in the E. coli. The calcium binding nature was established by performing various staining methods such as ruthenium red and stains-all. (45)Ca overlay method was also done to further support the data. Since the 3a protein forms ion channels, we were interested to see any conformational changes occurring in the Cyot3a upon calcium binding, using fluorescence spectroscopy and circular dichroism. These studies clearly indicate a significant change in the conformation of the Cyto3a protein after binding with calcium. Our results strongly suggest that the cytoplasmic domain of the 3a protein of SARS-CoV binds calcium in vitro, causing a change in protein conformation. </AbstractText><CopyrightInformation>Copyright © 2014 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Minakshi</LastName><ForeName>Rinki</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>International Centre for Genetic Engineering and Biotechnology, New Delhi, India; Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India. Electronic address: rinki.minakshi@hotmail.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Padhan</LastName><ForeName>Kartika</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>International Centre for Genetic Engineering and Biotechnology, New Delhi, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rehman</LastName><ForeName>Safikur</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hassan</LastName><ForeName>Md Imtaiyaz</ForeName><Initials>MI</Initials><AffiliationInfo><Affiliation>Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ahmad</LastName><ForeName>Faizan</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>08</Month><Day>10</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Virus Res</MedlineTA><NlmUniqueID>8410979</NlmUniqueID><ISSNLinking>0168-1702</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C487105">3a protein, severe acute respiratory syndrome coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>SY7Q814VUP</RegistryNumber><NameOfSubstance UI="D002118">Calcium</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002118" MajorTopicYN="N">Calcium</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003593" MajorTopicYN="N">Cytoplasm</DescriptorName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein 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