Structural properties of potexvirus coat proteins detected by optical methods
It has been shown by X-ray analysis that cores of coat proteins (CPs) from three potexviruses, flexible helical RNA-containing plant viruses, have similar α-helical structure. However, this similarity cannot explain structural lability of potexvirus virions, which is believed to determine their biol...
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| Veröffentlicht in: | Biochemistry (Moscow) 2016-12, Vol.81 (12), p.1522-1530 |
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| container_title | Biochemistry (Moscow) |
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| creator | Semenyuk, P. I. Karpova, O. V. Ksenofontov, A. L. Kalinina, N. O. Dobrov, E. N. Makarov, V. V. |
| description | It has been shown by X-ray analysis that cores of coat proteins (CPs) from three potexviruses, flexible helical RNA-containing plant viruses, have similar α-helical structure. However, this similarity cannot explain structural lability of potexvirus virions, which is believed to determine their biological activity. Here, we used circular dichroism (CD) spectroscopy in the far UV region to compare optical properties of CPs from three potexviruses with the same morphology and similar structure. CPs from
Alternanthera
mosaic virus (AltMV), potato aucuba mosaic virus (PAMV), and potato virus X (PVX) have been studied in a free state and in virions. The CD spectrum of AltMV virions was similar to the previously obtained CD spectrum of papaya mosaic virus (PapMV) virions, but differed significantly from the CD spectrum of PAMV virions. The CD spectrum of PAMV virions resembled in its basic characteristics the CD spectrum of PVX virions characterized by molar ellipticity that is abnormally low for α-helical proteins. Homology modeling of the CP structures in AltMV, PAMV, and PVX virions was based on the known high-resolution structures of CPs from papaya mosaic virus and bamboo mosaic virus and confirmed that the structures of the CP cores in all three viruses were nearly identical. Comparison of amino acid sequences of different potexvirus CPs and prediction of unstructured regions in these proteins revealed a possible correlation between specific features in the virion CD spectra and the presence of disordered N-terminal segments in the CPs. |
| doi_str_mv | 10.1134/S0006297916120130 |
| format | Article |
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Alternanthera
mosaic virus (AltMV), potato aucuba mosaic virus (PAMV), and potato virus X (PVX) have been studied in a free state and in virions. The CD spectrum of AltMV virions was similar to the previously obtained CD spectrum of papaya mosaic virus (PapMV) virions, but differed significantly from the CD spectrum of PAMV virions. The CD spectrum of PAMV virions resembled in its basic characteristics the CD spectrum of PVX virions characterized by molar ellipticity that is abnormally low for α-helical proteins. Homology modeling of the CP structures in AltMV, PAMV, and PVX virions was based on the known high-resolution structures of CPs from papaya mosaic virus and bamboo mosaic virus and confirmed that the structures of the CP cores in all three viruses were nearly identical. Comparison of amino acid sequences of different potexvirus CPs and prediction of unstructured regions in these proteins revealed a possible correlation between specific features in the virion CD spectra and the presence of disordered N-terminal segments in the CPs.</description><identifier>ISSN: 0006-2979</identifier><identifier>EISSN: 1608-3040</identifier><identifier>DOI: 10.1134/S0006297916120130</identifier><identifier>PMID: 28259129</identifier><language>eng</language><publisher>Moscow: Pleiades Publishing</publisher><subject>Alphaflexiviridae ; Alternanthera ; Amino Acid Sequence ; Amino acids ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Bioorganic Chemistry ; Capsid Proteins - chemistry ; Capsid Proteins - ultrastructure ; Circular Dichroism ; Conserved Sequence ; Cores ; Life Sciences ; Microbiology ; Models, Molecular ; Nicotiana - virology ; Optical properties ; Potato virus X ; Potatoes ; Potexvirus ; Potexvirus - ultrastructure ; Potyviridae ; Protein Conformation, alpha-Helical ; Protein Structure, Quaternary ; Proteins ; Regular Papers ; Ribonucleic acid ; RNA ; Structural Homology, Protein ; Virion - chemistry ; Virion - ultrastructure ; Viruses</subject><ispartof>Biochemistry (Moscow), 2016-12, Vol.81 (12), p.1522-1530</ispartof><rights>Pleiades Publishing, Ltd. 2016</rights><rights>COPYRIGHT 2016 Springer</rights><rights>Biochemistry (Moscow) is a copyright of Springer, 2016.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c472t-8e444e03b1a978c7a5ae177957ed19c8bae7fda4713808f977eca66a6b0648893</citedby><cites>FETCH-LOGICAL-c472t-8e444e03b1a978c7a5ae177957ed19c8bae7fda4713808f977eca66a6b0648893</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1134/S0006297916120130$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1134/S0006297916120130$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28259129$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Semenyuk, P. I.</creatorcontrib><creatorcontrib>Karpova, O. V.</creatorcontrib><creatorcontrib>Ksenofontov, A. L.</creatorcontrib><creatorcontrib>Kalinina, N. O.</creatorcontrib><creatorcontrib>Dobrov, E. N.</creatorcontrib><creatorcontrib>Makarov, V. V.</creatorcontrib><title>Structural properties of potexvirus coat proteins detected by optical methods</title><title>Biochemistry (Moscow)</title><addtitle>Biochemistry Moscow</addtitle><addtitle>Biochemistry (Mosc)</addtitle><description>It has been shown by X-ray analysis that cores of coat proteins (CPs) from three potexviruses, flexible helical RNA-containing plant viruses, have similar α-helical structure. However, this similarity cannot explain structural lability of potexvirus virions, which is believed to determine their biological activity. Here, we used circular dichroism (CD) spectroscopy in the far UV region to compare optical properties of CPs from three potexviruses with the same morphology and similar structure. CPs from
Alternanthera
mosaic virus (AltMV), potato aucuba mosaic virus (PAMV), and potato virus X (PVX) have been studied in a free state and in virions. The CD spectrum of AltMV virions was similar to the previously obtained CD spectrum of papaya mosaic virus (PapMV) virions, but differed significantly from the CD spectrum of PAMV virions. The CD spectrum of PAMV virions resembled in its basic characteristics the CD spectrum of PVX virions characterized by molar ellipticity that is abnormally low for α-helical proteins. Homology modeling of the CP structures in AltMV, PAMV, and PVX virions was based on the known high-resolution structures of CPs from papaya mosaic virus and bamboo mosaic virus and confirmed that the structures of the CP cores in all three viruses were nearly identical. Comparison of amino acid sequences of different potexvirus CPs and prediction of unstructured regions in these proteins revealed a possible correlation between specific features in the virion CD spectra and the presence of disordered N-terminal segments in the CPs.</description><subject>Alphaflexiviridae</subject><subject>Alternanthera</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Bioorganic Chemistry</subject><subject>Capsid Proteins - chemistry</subject><subject>Capsid Proteins - ultrastructure</subject><subject>Circular Dichroism</subject><subject>Conserved Sequence</subject><subject>Cores</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>Models, Molecular</subject><subject>Nicotiana - virology</subject><subject>Optical properties</subject><subject>Potato virus X</subject><subject>Potatoes</subject><subject>Potexvirus</subject><subject>Potexvirus - ultrastructure</subject><subject>Potyviridae</subject><subject>Protein Conformation, alpha-Helical</subject><subject>Protein Structure, Quaternary</subject><subject>Proteins</subject><subject>Regular Papers</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>Structural Homology, Protein</subject><subject>Virion - chemistry</subject><subject>Virion - ultrastructure</subject><subject>Viruses</subject><issn>0006-2979</issn><issn>1608-3040</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqNkV9P1jAUxhuCkRf0A3hjlnDjzfD0z9b2khAFEowXwPXSdWdQsq2z7Yx8e7u8iAqakF407fN7npyTh5B3FI4o5eLjJQDUTEtNa8qActghG1qDKjkI2CWbVS5XfY_sx3iXnww0f032mGKVpkxvyJfLFBablmCGYg5-xpAcxsL3xewT_vjuwhIL601a1YRuikWHCW3CrmjvCz8nZ7N1xHTru_iGvOrNEPHtw31Arj9_ujo5Ky--np6fHF-UVkiWSoVCCATeUqOlstJUBqmUupLYUW1Va1D2nRGScgWq11KiNXVt6hZqoZTmB-TDNjcP9W3BmJrRRYvDYCb0S2yokkKqDIsXoJUWWgFnGT18gt75JUx5kUxlhoPk8Ju6MQM2bup9Csauoc1xJZQQtFIqU0f_oPLpcHTWT9i7_P-XgW4NNvgYA_bNHNxown1DoVnbbp61nT3vHwZe2hG7R8evejPAtkDM0nSD4Y-N_pv6E6jCsTU</recordid><startdate>20161201</startdate><enddate>20161201</enddate><creator>Semenyuk, P. 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I.</au><au>Karpova, O. V.</au><au>Ksenofontov, A. L.</au><au>Kalinina, N. O.</au><au>Dobrov, E. N.</au><au>Makarov, V. V.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural properties of potexvirus coat proteins detected by optical methods</atitle><jtitle>Biochemistry (Moscow)</jtitle><stitle>Biochemistry Moscow</stitle><addtitle>Biochemistry (Mosc)</addtitle><date>2016-12-01</date><risdate>2016</risdate><volume>81</volume><issue>12</issue><spage>1522</spage><epage>1530</epage><pages>1522-1530</pages><issn>0006-2979</issn><eissn>1608-3040</eissn><abstract>It has been shown by X-ray analysis that cores of coat proteins (CPs) from three potexviruses, flexible helical RNA-containing plant viruses, have similar α-helical structure. However, this similarity cannot explain structural lability of potexvirus virions, which is believed to determine their biological activity. Here, we used circular dichroism (CD) spectroscopy in the far UV region to compare optical properties of CPs from three potexviruses with the same morphology and similar structure. CPs from
Alternanthera
mosaic virus (AltMV), potato aucuba mosaic virus (PAMV), and potato virus X (PVX) have been studied in a free state and in virions. The CD spectrum of AltMV virions was similar to the previously obtained CD spectrum of papaya mosaic virus (PapMV) virions, but differed significantly from the CD spectrum of PAMV virions. The CD spectrum of PAMV virions resembled in its basic characteristics the CD spectrum of PVX virions characterized by molar ellipticity that is abnormally low for α-helical proteins. Homology modeling of the CP structures in AltMV, PAMV, and PVX virions was based on the known high-resolution structures of CPs from papaya mosaic virus and bamboo mosaic virus and confirmed that the structures of the CP cores in all three viruses were nearly identical. Comparison of amino acid sequences of different potexvirus CPs and prediction of unstructured regions in these proteins revealed a possible correlation between specific features in the virion CD spectra and the presence of disordered N-terminal segments in the CPs.</abstract><cop>Moscow</cop><pub>Pleiades Publishing</pub><pmid>28259129</pmid><doi>10.1134/S0006297916120130</doi><tpages>9</tpages></addata></record> |
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| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Alphaflexiviridae Alternanthera Amino Acid Sequence Amino acids Biochemistry Biomedical and Life Sciences Biomedicine Bioorganic Chemistry Capsid Proteins - chemistry Capsid Proteins - ultrastructure Circular Dichroism Conserved Sequence Cores Life Sciences Microbiology Models, Molecular Nicotiana - virology Optical properties Potato virus X Potatoes Potexvirus Potexvirus - ultrastructure Potyviridae Protein Conformation, alpha-Helical Protein Structure, Quaternary Proteins Regular Papers Ribonucleic acid RNA Structural Homology, Protein Virion - chemistry Virion - ultrastructure Viruses |
| title | Structural properties of potexvirus coat proteins detected by optical methods |
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