Amino acids of conserved kinase motifs of cytomegalovirus protein UL97 are essential for autophosphorylation.

Abstract:

:Thirteen point mutations targeting predicted domains conserved in homologous protein kinases were introduced into the UL97 coding region of the human cytomegalovirus. All mutagenized proteins were expressed in cells infected with recombinant vaccinia viruses (rVV). Several mutations drastically reduced ganciclovir (GCV) phosphorylation. Mutations at amino acids G340, A442, L446, and F523 resulted in a complete loss of pUL97 phosphorylation, which was strictly associated with a loss of GCV phosphorylation. Our results confirm that in rVV-infected cells pUL97 phosphorylation is due to autophosphorylation and show that several amino acids conserved within domains of protein kinases are essential for this pUL97 phosphorylation. GCV phosphorylation is dependent on pUL97 phosphorylation.

journal_name

J Virol

journal_title

Journal of virology

authors

Michel D,Kramer S,Höhn S,Schaarschmidt P,Wunderlich K,Mertens T

doi

10.1128/JVI.73.10.8898-8901.1999

subject

Has Abstract

pub_date

1999-10-01 00:00:00

pages

8898-901

issue

10

eissn

0022-538X

issn

1098-5514

journal_volume

73

pub_type

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