Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Gene Review:

ECs1635 - major capsid protein

Escherichia coli O157:H7 str. Sakai

Chee, M. et al., Fokine, A. et al., Keppel, F. et al., Kulski, J.K. et al., García-Escudero, R. et al., et al.

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of ECs1635

Several large, lytic bacteriophages, such as T4 and RB49, use the host-encoded GroEL in conjunction with their own bacteriophage-encoded cochaperonin for the correct assembly of their major capsid protein, suggesting a cochaperonin specificity for the in vivo folding of certain substrates [1].
Identification of the major capsid protein gene of human cytomegalovirus [2].
The obtained antisera reacted in Western immunoblots with the MCP of purified HCMV virions [2].
Inducible gene expression from African swine fever virus recombinants: analysis of the major capsid protein p72 [3].
The coding region for the major capsid protein (MCP) of human cytomegalovirus (HCMV) was identified by comparing the protein sequence with the respective sequences of herpes simplex virus (HSV), Epstein-Barr virus, and varicella-zoster virus [2].

High impact information on ECs1635

Mouse monoclonal antibodies (mAbs) were raised against the major capsid protein, L1, of human papillomavirus type 16 (HPV16), produced in Escherichia coli with the expression plasmid pTrcL1 [4].
A deletion and point mutation study of the human papillomavirus type 16 major capsid gene [5].

Analytical, diagnostic and therapeutic context of ECs1635

The structure of such a mutant virus, determined by cryo-electron microscopy to 26 angstroms, shows that the gp24 pentamers are replaced by mutant major capsid protein (gp23) pentamers at the vertices, thus re-creating a viral capsid prior to the evolution of specialized major capsid proteins and vertex proteins [6].

References

Bacteriophage-encoded cochaperonins can substitute for Escherichia coli's essential GroES protein. Keppel, F., Rychner, M., Georgopoulos, C. EMBO Rep. (2002) [Pubmed]
Identification of the major capsid protein gene of human cytomegalovirus. Chee, M., Rudolph, S.A., Plachter, B., Barrell, B., Jahn, G. J. Virol. (1989) [Pubmed]
Inducible gene expression from African swine fever virus recombinants: analysis of the major capsid protein p72. García-Escudero, R., Andrés, G., Almazán, F., Viñuela, E. J. Virol. (1998) [Pubmed]
Type specific and genotype cross reactive B epitopes of the L1 protein of HPV16 defined by a panel of monoclonal antibodies. Kulski, J.K., Sadleir, J.W., Kelsall, S.R., Cicchini, M.S., Shellam, G., Peng, S.W., Qi, Y.M., Galloway, D.A., Zhou, J., Frazer, I.H. Virology (1998) [Pubmed]
A deletion and point mutation study of the human papillomavirus type 16 major capsid gene. Varsani, A., Williamson, A.L., Jaffer, M.A., Rybicki, E.P. Virus Res. (2006) [Pubmed]
Cryo-EM structure of a bacteriophage T4 gp24 bypass mutant: the evolution of pentameric vertex proteins in icosahedral viruses. Fokine, A., Battisti, A.J., Kostyuchenko, V.A., Black, L.W., Rossmann, M.G. J. Struct. Biol. (2006) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use

[search][advanced]