Crystal Structure of Glycoprotein B from Herpes Simplex Virus 1

American Association for the Advancement of Science (AAAS) - Tập 313 Số 5784 - Trang 217-220 - 2006
Ekaterina E. Heldwein1,2,3,4,5, Huan Lou2,3,4,5, Florent C. Bender2,3,4,5, Gary H. Cohen2,3,4,5, Roselyn J. Eisenberg2,3,4,5, Stephen C. Harrison1,2,3,4,5
1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 320 Longwood Avenue, Boston, MA 02115, USA.
2Department of Microbiology, School of Dental Medicine, University of Pennsylvania, 240 South 40th Street, Philadelphia, PA 19104, USA.
3Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, 240 South 40th Street, Philadelphia, PA 19104, USA.
4Howard Hughes Medical Institute, Children’s Hospital, 320, Longwood Avenue, Boston, MA 02115, USA
5Laboratory of Molecular Medicine, 320 Longwood Avenue, Boston, MA 02115, USA.

Tóm tắt

Glycoprotein B (gB) is the most conserved component of the complex cell-entry machinery of herpes viruses. A crystal structure of the gB ectodomain from herpes simplex virus type 1 reveals a multidomain trimer with unexpected homology to glycoprotein G from vesicular stomatitis virus (VSV G). An α-helical coiled-coil core relates gB to class I viral membrane fusion glycoproteins; two extended β hairpins with hydrophobic tips, homologous to fusion peptides in VSV G, relate gB to class II fusion proteins. Members of both classes accomplish fusion through a large-scale conformational change, triggered by a signal from a receptor-binding component. The domain connectivity within a gB monomer would permit such a rearrangement, including long-range translocations linked to viral and cellular membranes.

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Tài liệu tham khảo

10.1128/jvi.62.8.2596-2604.1988

10.1128/jvi.62.5.1486-1494.1988

10.1128/jvi.66.1.341-348.1992

10.1128/jvi.67.4.2285-2297.1993

10.1128/JVI.77.19.10179-10185.2003

10.1111/j.1462-5822.2004.00389.x

10.1016/S1097-2765(01)00298-2

10.1038/sj.emboj.7600875

10.1016/j.virol.2004.03.024

10.1073/pnas.0401883101

10.1128/jvi.67.4.2191-2201.1993

10.1006/viro.2001.1004

10.1016/0042-6822(84)90022-9

Materials and methods are available as supporting material on Science Online.

10.1126/science.1127683

10.1128/jvi.70.11.7379-7387.1996

10.1016/S0968-0004(99)01472-3

10.1042/bj3500001

10.1016/S0968-0004(00)89105-7

10.1016/S0042-6822(95)80002-6

10.1128/jvi.63.2.730-738.1989

10.1128/JVI.79.7.4066-4079.2005

10.1128/JVI.72.7.6119-6130.1998

10.1074/jbc.270.29.17575

10.1016/S0065-3527(05)64007-9

Single-letter abbreviations for the amino acid residues are as follows: A Ala; C Cys; D Asp; E Glu; F Phe; G Gly; H His; I Ile; K Lys; L Leu; M Met; N Asn; P Pro; Q Gln; R Arg; S Ser; T Thr; V Val; W Trp; and Y Tyr.

10.1107/S0021889891004399

More information is available online (http://quorum.tamu.edu/Manual/Manual/Manual.html).

G. J. Kleywegt, T. A. Jones, Acta Crystallogr.D52, 826 (1996).

10.1128/jvi.53.1.243-253.1985

10.1016/0042-6822(88)90513-2

10.1016/0042-6822(89)90102-5

10.1128/jvi.63.5.1995-2001.1989

10.1128/jvi.67.2.703-710.1993

We thank M. Berne of the Tufts Protein Chemistry Facility for N-terminal sequencing D. King of the University of California at Berkeley for mass spectrometry E. Settembre for the x-ray data collection E. M. Vogan for help with crystallographic software and L. Pereira for providing several antibodies to gB. This work was funded by NIH grants AI065886 (to E.E.H.) AI049980 (to S.C.H.) and AI056045 and NS36731 (to R.J.E.). S.C.H. is an investigator in the Howard Hughes Medical Institute. Coordinates and structure factors have been deposited with the Research Collaboratory for Structural Bioinformatics (RCSB) Protein Data Bank (PDB) with accession code 2gum.

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American Association for the Advancement of Science (AAAS)

Tập 313 Số 5784

217-220

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