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Conserved Receptor-binding Domains of Lake Victoria Marburgvirus and Zaire Ebolavirus Bind a Common Receptor.

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Title: Conserved Receptor-binding Domains of Lake Victoria Marburgvirus and Zaire Ebolavirus Bind a Common Receptor.
Authors: Kuhn, Jens H.1,2, Radoshitzky, Shell R.1, Guth, Alexander C.1, Warfield, Kelly L.3, Wenhui Li1, Vincent, Martin J.4, Towner, Jonathan S.4, Nichol, Stuart T.4, Bavari, Sina3, Choe, Hyeryun5, Aman, M. Javad3, Farzan, Michael1 farzan@hms.harvard.edu
Source: Journal of Biological Chemistry. 6/9/2006, Vol. 281 Issue 23, p15951-15958. 8p. 6 Graphs.
Subjects: Glycoproteins, Glycoconjugates, Cell culture, Tissue-specific antigens, Preventive medicine, Vaccination, RNA viruses
Abstract: The GP1,2 envelope glycoproteins (GP) of filoviruses (marburg- and ebolaviruses) mediate cell-surface attachment, membrane fusion, and entry into permissive cells. Here we show that a 151-amino acid fragment of the Lake Victoria marburgvirus GP1 subunit bound filovirus-permissive cell lines more efficiently than full-length GP1. An homologous 148-amino acid fragment of the Zaire ebolavirus GP1 subunit similarly bound the same cell lines more efficiently than a series of longer GP1 truncation variants. Neither the marburgvirus GP1 fragment nor that of ebolavirus bound a nonpermissive lymphocyte cell line. Both fragments specifically inhibited replication of infectious Zaire ebolavirus, as well as entry of retroviruses pseudotyped with either Lake Victoria marburgvirus or Zaire ebolavirus GP1,2. These studies identify the receptor-binding domains of both viruses, indicate that these viruses utilize a common receptor, and suggest that a single small molecule or vaccine can be developed to inhibit infection of all filoviruses. [ABSTRACT FROM AUTHOR]
Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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DbLabel: Engineering Source
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PubType: Academic Journal
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  Data: Conserved Receptor-binding Domains of Lake Victoria Marburgvirus and Zaire Ebolavirus Bind a Common Receptor.
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  Data: <searchLink fieldCode="AR" term="%22Kuhn%2C+Jens+H%2E%22">Kuhn, Jens H.</searchLink><relatesTo>1,2</relatesTo><br /><searchLink fieldCode="AR" term="%22Radoshitzky%2C+Shell+R%2E%22">Radoshitzky, Shell R.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Guth%2C+Alexander+C%2E%22">Guth, Alexander C.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Warfield%2C+Kelly+L%2E%22">Warfield, Kelly L.</searchLink><relatesTo>3</relatesTo><br /><searchLink fieldCode="AR" term="%22Wenhui+Li%22">Wenhui Li</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Vincent%2C+Martin+J%2E%22">Vincent, Martin J.</searchLink><relatesTo>4</relatesTo><br /><searchLink fieldCode="AR" term="%22Towner%2C+Jonathan+S%2E%22">Towner, Jonathan S.</searchLink><relatesTo>4</relatesTo><br /><searchLink fieldCode="AR" term="%22Nichol%2C+Stuart+T%2E%22">Nichol, Stuart T.</searchLink><relatesTo>4</relatesTo><br /><searchLink fieldCode="AR" term="%22Bavari%2C+Sina%22">Bavari, Sina</searchLink><relatesTo>3</relatesTo><br /><searchLink fieldCode="AR" term="%22Choe%2C+Hyeryun%22">Choe, Hyeryun</searchLink><relatesTo>5</relatesTo><br /><searchLink fieldCode="AR" term="%22Aman%2C+M%2E+Javad%22">Aman, M. Javad</searchLink><relatesTo>3</relatesTo><br /><searchLink fieldCode="AR" term="%22Farzan%2C+Michael%22">Farzan, Michael</searchLink><relatesTo>1</relatesTo><i> farzan@hms.harvard.edu</i>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Biological+Chemistry%22">Journal of Biological Chemistry</searchLink>. 6/9/2006, Vol. 281 Issue 23, p15951-15958. 8p. 6 Graphs.
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  Data: <searchLink fieldCode="DE" term="%22Glycoproteins%22">Glycoproteins</searchLink><br /><searchLink fieldCode="DE" term="%22Glycoconjugates%22">Glycoconjugates</searchLink><br /><searchLink fieldCode="DE" term="%22Cell+culture%22">Cell culture</searchLink><br /><searchLink fieldCode="DE" term="%22Tissue-specific+antigens%22">Tissue-specific antigens</searchLink><br /><searchLink fieldCode="DE" term="%22Preventive+medicine%22">Preventive medicine</searchLink><br /><searchLink fieldCode="DE" term="%22Vaccination%22">Vaccination</searchLink><br /><searchLink fieldCode="DE" term="%22RNA+viruses%22">RNA viruses</searchLink>
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  Data: The GP1,2 envelope glycoproteins (GP) of filoviruses (marburg- and ebolaviruses) mediate cell-surface attachment, membrane fusion, and entry into permissive cells. Here we show that a 151-amino acid fragment of the Lake Victoria marburgvirus GP1 subunit bound filovirus-permissive cell lines more efficiently than full-length GP1. An homologous 148-amino acid fragment of the Zaire ebolavirus GP1 subunit similarly bound the same cell lines more efficiently than a series of longer GP1 truncation variants. Neither the marburgvirus GP1 fragment nor that of ebolavirus bound a nonpermissive lymphocyte cell line. Both fragments specifically inhibited replication of infectious Zaire ebolavirus, as well as entry of retroviruses pseudotyped with either Lake Victoria marburgvirus or Zaire ebolavirus GP1,2. These studies identify the receptor-binding domains of both viruses, indicate that these viruses utilize a common receptor, and suggest that a single small molecule or vaccine can be developed to inhibit infection of all filoviruses. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1074/jbc.M601796200
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      – SubjectFull: Glycoproteins
        Type: general
      – SubjectFull: Glycoconjugates
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      – SubjectFull: Cell culture
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      – SubjectFull: Tissue-specific antigens
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      – SubjectFull: Preventive medicine
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      – SubjectFull: RNA viruses
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              Text: 6/9/2006
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