Α-helical coiled-coil structures of trypanosoma brucei variable surface glycoproteins

Α-helical coiled-coil structures of trypanosoma brucei variable surface glycoproteins

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ABSTRACT We have used electron microscopy to examine purified intact variable surface glycoproteins (VSGs) from clones derived from two distinct stocks of _Trypanosoma brucei_. The VSG molecule from MITat 1.2 has a large elongated domain consistent with the shape of the dimeric N-terminal domain determined by X-ray analysis (see preceding paper1), and a heretofore unseen short, thin fibrous tail presumed to be the C-terminal domain. Electron microscopy on DiTat 1.3, however, indicates a morphology quite distinct from that of MITat 1.2. Analysis of four VSG amino acid sequences reveals 7-fold periodicities (heptad repeats) which indicate that _α_-helical coiled-coil secondary structure elements occur in all of these VSGs, consistent with the observation of helical bundles in one VSG1. These results suggest the possibility that VSG antigenic diversity may be related to a diversity in length and disposition of _α_-helical bundles and coiled-coil domains. Access through your institution Buy or subscribe This is a preview of subscription content, access via your institution ACCESS OPTIONS Access through your institution Subscribe to this journal Receive 51 print issues and online access $199.00 per year only $3.90 per issue Learn more Buy this article * Purchase on SpringerLink * Instant access to full article PDF Buy now Prices may be subject to local taxes which are calculated during checkout ADDITIONAL ACCESS OPTIONS: * Log in * Learn about institutional subscriptions * Read our FAQs * Contact customer support SIMILAR CONTENT BEING VIEWED BY OTHERS THE STRUCTURE OF _SHIGELLA_ VIRUS SF14 REVEALS THE PRESENCE OF TWO DECORATION PROTEINS AND TWO LONG TAIL FIBERS Article Open access 12 February 2025 IN SITU STRUCTURE AND ORGANIZATION OF THE INFLUENZA C VIRUS SURFACE GLYCOPROTEIN Article Open access 16 March 2021 CRYO-EM STRUCTURE OF SEVERE FEVER WITH THROMBOCYTOPENIA SYNDROME VIRUS Article Open access 10 October 2023 REFERENCES * Freymann, D., Metcalf, P., Turner, M. & Wiley, D. C. _Nature_ 310, 167–169 (1984). Article  ADS  Google Scholar  * Holder, A. A. & Cross, G. A. M. _Molec. biochem. Parasit._ 2, 135–150 (1981). Article  CAS  Google Scholar  * Rice-Ficht, A. C., Chen, K. C. & Donelson, J. E. _Nature_ 294, 53–57 (1981). Article  ADS  CAS  Google Scholar  * Allen, G., Gurnett, L. P. & Cross, G. A. M. _J. molec. Biol._ 157, 527–546 (1982). Article  CAS  Google Scholar  * Pays, E. _et al._ _Cell_ 34, 371–381 (1983). Article  CAS  Google Scholar  * Rice-Ficht, A. C., Chen, K. C. & Donelson, J. E. _Nature_ 298, 676–679 (1982). Article  ADS  CAS  Google Scholar  * Donelson, J. E., Young, J. R., Dorfman, D., Majiwa, P. A. O. & Williams, R. O. _Nucleic Acids Res._ 10, 6581–6595 (1982). Article  CAS  Google Scholar  * Chou, P. Y. & Fasman, G. D. _A. Rev. Biochem._ 47, 251–276 (1978). Article  CAS  Google Scholar  * Robson, B. & Suzuki, E. _J. molec. Biol._ 107, 327–356 (1976). Article  CAS  Google Scholar  * Garnier, J., Osguthrope, D. J. & Robson, B. _J. molec. Biol._ 120, 97–120 (1978). Article  CAS  Google Scholar  * Parry, D. A. D. in _Fibrous Proteins: Scientific, Industrial and Medical Aspects_ Vol. 1 (eds Parry, D. A. D. & Creamer, L. K.) 393–427 (Academic, London, 1979). Google Scholar  * Parry, D. A. D. _Biosci. Rep._ 2, 1017–1024 (1982). Article  CAS  Google Scholar  * Crick, F. H. C. _Acta crystallogr._ 6, 689–697 (1953). Article  CAS  Google Scholar  * Weber, P. C. & Salemme, F. R. _Nature_ 287, 82–84 (1980). Article  ADS  CAS  Google Scholar  * Lalor, T. M. _et al._ _Proc. natn. Acad. Sci. U.S.A._ 81, 998–1002 (1984). Article  ADS  CAS  Google Scholar  * Cohen, C. & Phillips, G. N. Jr _Proc. natn. Acad. Sci. U.S.A._ 78, 5303–5304 (1981). Article  ADS  CAS  Google Scholar  * Flicker, P. F., Wallimann, T. & Vibert, P. _J. molec. Biol._ 169, 723–741 (1983). Article  CAS  Google Scholar  * Cross, G. A. M. _Parasitology_ 71, 393–417 (1975). Article  CAS  Google Scholar  * Roelants, G. E. _et al._ _Expl Parasit._ (submitted). Download references AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts, 02254, USA Carolyn Cohen & Bruce Reinhardt * Department of Chemistry, Biochemistry and Biophysics, Massey University, Palmerston North, New Zealand David A. D. Parry * Centre de Recherches sur les Trypanosomoses Animales, Bobo-Dioulasso, Haute-Volta Georges E. Roelants, Wolfgang Hirsch & Babine Kanwé Authors * Carolyn Cohen View author publications You can also search for this author inPubMed Google Scholar * Bruce Reinhardt View author publications You can also search for this author inPubMed Google Scholar * David A. D. Parry View author publications You can also search for this author inPubMed Google Scholar * Georges E. Roelants View author publications You can also search for this author inPubMed Google Scholar * Wolfgang Hirsch View author publications You can also search for this author inPubMed Google Scholar * Babine Kanwé View author publications You can also search for this author inPubMed Google Scholar RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Cohen, C., Reinhardt, B., Parry, D. _et al._ _α_-Helical coiled-coil structures of _Trypanosoma brucei_ variable surface glycoproteins. _Nature_ 311, 169–171 (1984). https://doi.org/10.1038/311169a0 Download citation * Received: 18 June 1984 * Accepted: 05 July 1984 * Issue Date: 13 September 1984 * DOI: https://doi.org/10.1038/311169a0 SHARE THIS ARTICLE Anyone you share the following link with will be able to read this content: Get shareable link Sorry, a shareable link is not currently available for this article. Copy to clipboard Provided by the Springer Nature SharedIt content-sharing initiative

ABSTRACT We have used electron microscopy to examine purified intact variable surface glycoproteins (VSGs) from clones derived from two distinct stocks of _Trypanosoma brucei_. The VSG


molecule from MITat 1.2 has a large elongated domain consistent with the shape of the dimeric N-terminal domain determined by X-ray analysis (see preceding paper1), and a heretofore unseen


short, thin fibrous tail presumed to be the C-terminal domain. Electron microscopy on DiTat 1.3, however, indicates a morphology quite distinct from that of MITat 1.2. Analysis of four VSG


amino acid sequences reveals 7-fold periodicities (heptad repeats) which indicate that _α_-helical coiled-coil secondary structure elements occur in all of these VSGs, consistent with the


observation of helical bundles in one VSG1. These results suggest the possibility that VSG antigenic diversity may be related to a diversity in length and disposition of _α_-helical bundles


and coiled-coil domains. Access through your institution Buy or subscribe This is a preview of subscription content, access via your institution ACCESS OPTIONS Access through your


institution Subscribe to this journal Receive 51 print issues and online access $199.00 per year only $3.90 per issue Learn more Buy this article * Purchase on SpringerLink * Instant access


to full article PDF Buy now Prices may be subject to local taxes which are calculated during checkout ADDITIONAL ACCESS OPTIONS: * Log in * Learn about institutional subscriptions * Read our


FAQs * Contact customer support SIMILAR CONTENT BEING VIEWED BY OTHERS THE STRUCTURE OF _SHIGELLA_ VIRUS SF14 REVEALS THE PRESENCE OF TWO DECORATION PROTEINS AND TWO LONG TAIL FIBERS


Article Open access 12 February 2025 IN SITU STRUCTURE AND ORGANIZATION OF THE INFLUENZA C VIRUS SURFACE GLYCOPROTEIN Article Open access 16 March 2021 CRYO-EM STRUCTURE OF SEVERE FEVER WITH


THROMBOCYTOPENIA SYNDROME VIRUS Article Open access 10 October 2023 REFERENCES * Freymann, D., Metcalf, P., Turner, M. & Wiley, D. C. _Nature_ 310, 167–169 (1984). Article  ADS  Google


Scholar  * Holder, A. A. & Cross, G. A. M. _Molec. biochem. Parasit._ 2, 135–150 (1981). Article  CAS  Google Scholar  * Rice-Ficht, A. C., Chen, K. C. & Donelson, J. E. _Nature_


294, 53–57 (1981). Article  ADS  CAS  Google Scholar  * Allen, G., Gurnett, L. P. & Cross, G. A. M. _J. molec. Biol._ 157, 527–546 (1982). Article  CAS  Google Scholar  * Pays, E. _et


al._ _Cell_ 34, 371–381 (1983). Article  CAS  Google Scholar  * Rice-Ficht, A. C., Chen, K. C. & Donelson, J. E. _Nature_ 298, 676–679 (1982). Article  ADS  CAS  Google Scholar  *


Donelson, J. E., Young, J. R., Dorfman, D., Majiwa, P. A. O. & Williams, R. O. _Nucleic Acids Res._ 10, 6581–6595 (1982). Article  CAS  Google Scholar  * Chou, P. Y. & Fasman, G. D.


_A. Rev. Biochem._ 47, 251–276 (1978). Article  CAS  Google Scholar  * Robson, B. & Suzuki, E. _J. molec. Biol._ 107, 327–356 (1976). Article  CAS  Google Scholar  * Garnier, J.,


Osguthrope, D. J. & Robson, B. _J. molec. Biol._ 120, 97–120 (1978). Article  CAS  Google Scholar  * Parry, D. A. D. in _Fibrous Proteins: Scientific, Industrial and Medical Aspects_


Vol. 1 (eds Parry, D. A. D. & Creamer, L. K.) 393–427 (Academic, London, 1979). Google Scholar  * Parry, D. A. D. _Biosci. Rep._ 2, 1017–1024 (1982). Article  CAS  Google Scholar  *


Crick, F. H. C. _Acta crystallogr._ 6, 689–697 (1953). Article  CAS  Google Scholar  * Weber, P. C. & Salemme, F. R. _Nature_ 287, 82–84 (1980). Article  ADS  CAS  Google Scholar  *


Lalor, T. M. _et al._ _Proc. natn. Acad. Sci. U.S.A._ 81, 998–1002 (1984). Article  ADS  CAS  Google Scholar  * Cohen, C. & Phillips, G. N. Jr _Proc. natn. Acad. Sci. U.S.A._ 78,


5303–5304 (1981). Article  ADS  CAS  Google Scholar  * Flicker, P. F., Wallimann, T. & Vibert, P. _J. molec. Biol._ 169, 723–741 (1983). Article  CAS  Google Scholar  * Cross, G. A. M.


_Parasitology_ 71, 393–417 (1975). Article  CAS  Google Scholar  * Roelants, G. E. _et al._ _Expl Parasit._ (submitted). Download references AUTHOR INFORMATION AUTHORS AND AFFILIATIONS *


Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts, 02254, USA Carolyn Cohen & Bruce Reinhardt * Department of Chemistry, Biochemistry and


Biophysics, Massey University, Palmerston North, New Zealand David A. D. Parry * Centre de Recherches sur les Trypanosomoses Animales, Bobo-Dioulasso, Haute-Volta Georges E. Roelants, 


Wolfgang Hirsch & Babine Kanwé Authors * Carolyn Cohen View author publications You can also search for this author inPubMed Google Scholar * Bruce Reinhardt View author publications You


can also search for this author inPubMed Google Scholar * David A. D. Parry View author publications You can also search for this author inPubMed Google Scholar * Georges E. Roelants View


author publications You can also search for this author inPubMed Google Scholar * Wolfgang Hirsch View author publications You can also search for this author inPubMed Google Scholar *


Babine Kanwé View author publications You can also search for this author inPubMed Google Scholar RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Cohen,


C., Reinhardt, B., Parry, D. _et al._ _α_-Helical coiled-coil structures of _Trypanosoma brucei_ variable surface glycoproteins. _Nature_ 311, 169–171 (1984).


https://doi.org/10.1038/311169a0 Download citation * Received: 18 June 1984 * Accepted: 05 July 1984 * Issue Date: 13 September 1984 * DOI: https://doi.org/10.1038/311169a0 SHARE THIS


ARTICLE Anyone you share the following link with will be able to read this content: Get shareable link Sorry, a shareable link is not currently available for this article. Copy to clipboard


Provided by the Springer Nature SharedIt content-sharing initiative