Structure of the herpes simplex virus capsid: Peptide A862-H880 of the major capsid protein is displayed on the rim of the capsomer protrusions

Virology

Volumn 228, Issue 2, 1997, Pages 229-235

  Spencer, Juliet V ^a   Trus, Benes L ^b,c   Booy, Frank P ^c   Steven, Alasdair C ^c   Newcomb, William W ^a   Brown, Jay C ^a  

^a UNIVERSITY OF VIRGINIA HEALTH SYSTEM   (United States)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^c NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; MONOCLONAL ANTIBODY;

AMINO ACID SEQUENCE; ARTICLE; HERPES SIMPLEX VIRUS 1; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PURIFICATION; ULTRASTRUCTURE; VIRUS CAPSID; VIRUS MORPHOLOGY;

HERPES; HUMAN HERPESVIRUS 1; MIRIDAE; SIMPLEXVIRUS;

EID: 18544402853     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1996.8392     Document Type: Article

References (30)

1. Baker T. S., Cheng R. H. A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy. J. Struct. Biol. 116:1996;120-130.
2. Baker T. S., Newcomb W. W., Booy F. P., Brown J. C., Steven A. C. Three-dimensional structures of maturable and abortive capsids of equine herpesvirus 1 from cryoelectron microscopy. J. Virol. 64:1990;563-573.
3. Booy F. P., Trus B. L., Newcomb W. W., Brown J. C., Conway J. F., Steven A. C. Finding a needle in a haystack: Detection of a small protein (the 12-kDa VP26) in a large complex (the 200 MDa capsid of the herpes simplex virus). Proc. Natl. Acad. Sci. USA. 91:1994;5652-5656.
4. Chou P. Y., Fasman G. D. Prediction of protein conformation. Biochemistry. 13:1974;222-245.
5. Cicchetti P., Mayer B. J., Theil G., Baltimore D. Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho. Science. 257:1992;803-806.
6. Cohen G. B., Ren R., Baltimore D. Modular binding domains in signal transduction proteins. Cell. 80:1995;237-248.
7. Fane B. A., Hayashi M. Second-site suppressors of a cold sensitive prohead accessory protein of bacteriophage φX174. Genetics. 128:1991;663-671.
8. Francis N. R., Irikura V. M., Yamaguchi S., DeRosier D. J., Macnab R. M. Localization of theSalmonella typhimurium. Proc. Natl. Acad. Sci. USA. 89:1992;6304-6308.
9. Garnier J., Osguthorpe D. J., Robson B. Analysis of the accuracy and implications of a simple method for predicting the secondary structure of globular proteins. J. Mol. Biol. 120:1978;97-120.
10. Gibson W., Roizman B. Proteins specified by herpes simplex virus. VIII. Characterization and composition of multiple capsid forms of subtypes 1 and 2. J. Virol. 10:1972;1044-1052.
11. Harrison S. C., Olson A. J., Schutt C. E., Winkler F. K., Bricogne G. Tomato bushy stunt virus at 2.9 A resolution. Nature. 276:1978;368-373.
12. Ilag L. L., McKenna R., Yadav M. P., BeMiller J. N., Incardonna N. L., Rossman M. G. Calcium induced structural changes in bacteriophage φX174. J. Mol. Biol. 244:1994;291-300.
13. Liddington R. C., Yan Y., Moulai J., Sahli R., Benjamin T. L., Harrison S. C. Structure of simian virus 40 at 3.8-A resolution. Nature. 354:1991;278-284.
14. Newcomb W. W., Homa F. L., Thomsen D. R., Booy F. P., Trus B. L., Steven A. C., Spencer J. V., Brown J. C. Assembly of the herpes simplex virus capsid: Identification of intermediates in cell-free capsid formation. J. Mol. Biol. 263:1996;432-446.
15. Newcomb W. W., Trus B. L., Booy F. P., Steven A. C., Wall J. S., Brown J. C. Structure of the herpes simplex virus capsid: Molecular composition of the pentons and the triplexes. J. Mol. Biol. 232:1993;499-511.
16. Newcomb W. W., Brown J. C. Structure of the herpes simplex virus capsid: Effects of extraction with guanidine hydrochloride and partial reconstitution of extracted capsids. J. Virol. 65:1991;613-620.
17. Olson H. M., Nag B., Etchison J. R., Traut R. R., Glitz D. G. Differential localization of two epitopes ofEscherichia coli. J. Biol. Chem. 166:1991;1898-1902.
18. Pearson W. R., Lipman D. J. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA. 85:1988;2444-2448.
19. Perdue M. L., Cohen J. C., Kemp M. C., Randall C. C., O'Callaghan D. J. Characterization of three species of nucleocapsids of equine herpes virus type 1. Virology. 64:1975;187-205.
20. Ren R., Mayer B. J., Cicchetti P., Baltimore D. Identification of a ten-amino acid proline-rich SH3 binding site. Science. 259:1993;1157-1161.
21. Roizman B. Herpesviridae: A brief introduction. Virology. 1996;Lippincot-Raven, Philadelphia. p. 2231-2295.
22. Schrag J. D., Prasad B. V. V., Rixon F. J., Chiu W. Three-dimensional structure of the HSV1 nucleocapsid. Cell. 56:1989;651-660.
23. Smith T. J., Olson N. H., Cheng R. H., Chase E. S., Baker T. S. Structure of a human rhinovirus-bivalently bound antibody complex: Implication for viral neutralization and antibody flexibility. Proc. Natl. Acad Sci. USA. 90:1993;7015-7018.
24. Steven A. C., Bauer A. C., Bisher M. E., Robey F. A., Black L. W. The maturation-dependent conformational change of phage T4 capsid involves the translocation of specific epitopes between the inner and the outer capsid surfaces. J. Struct. Biol. 106:1991;221-236.
25. Steven A. C., Roberts C. R., Hay J., Bisher M. E., Pun M., Trus B. L. Hexavalent capsomers of herpes simplex virus type 2: symmetry, shape, dimensions and oligomeric status. J. Virol. 57:1986;578-584.
26. Trus B. L., Booy F. P., Newcomb W. W., Brown J. C., Homa F. L., Thomsen D. R., Steven A. C. The herpes simplex virus procapsid: structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly. J. Mol. Biol. 263:1996;447-462.
27. Trus B. L., Homa F. L., Booy F. P., Newcomb W. W., Thomsen D. R., Cheng N., Brown J. C., Steven A. C. Herpes simplex virus capsids assembled in insect cells infected with recombinant baculoviruses: Structural authenticity and localization of VP26. J. Virol. 69:1995;7362-7366.
28. Trus B. L., Newcomb W. W., Booy F. P., Brown J. C., Steven A. C. Distinct monoclonal antibodies separately label the hexons or the pentons of herpes simplex virus capsid. Proc. Natl. Acad. Sci. USA. 89:1992;11508-11512.
29. Zhou Z. H., He J., Jakana J., Tatman J. D., Rixon F. J., Chiu W. Assembly of VP26 in herpes simplex virus-1 inferred from structures of wild-type and recombinant capsids. Nature Struct. Biol. 2:1995;1026-1030.
30. Zhou Z. H., Prasad B. V. V., Jakana J., Rixon F. J., Chiu W. Protein subunit structures in the herpes simplex virus A-capsid determined from 400kV spot-scan electron cryomicroscopy. J. Mol. Biol. 242:1994;456-469.