Structural analysis of the US-segment of a viable temperature sensitive human cytomegalovirus mutant.
Structural analysis of the US-segment of a viable temperature sensitive human cytomegalovirus mutant (ts9) by the use of restriction enzymes, specific amplifications by the polymerase chain reaction and DNA sequencing, revealed deletions of open reading frames (orf) US14 and part of US15 in addition to that concerning US1 through US13 as reported previously [9]. It was further verified that the Hind III H-fragment and a major portion of the Hind III W-fragment were duplicated in inverted orientation. By the use of a monospecific antibody prepared against a procaryotic recombinant US11-specific product it was shown that the ts9 mutant was in fact deficient in a 30 kDa polypeptide, the gene product of orf US11.
Institut für Virologie der Philipps-Universität, Marburg, Federal Republic of Germany.
T
T
Mockenhaupt
M
M
Reschke
E
E
Bogner
B
B
Reis
K
K
Radsak
D001483:Base Sequence; D003587:Cytomegalovirus / Q000235:genetics* / Q000502:physiology*; D017931:DNA Primers; D004279:DNA, Viral / Q000737:chemistry / Q000378:metabolism; D015247:Deoxyribonuclease HindIII; D005347:Fibroblasts; D006801:Humans; D008969:Molecular Sequence Data; D017354:Point Mutation; D016133:Polymerase Chain Reaction; D015183:Restriction Mapping; D013696:Temperature; D014771:Virion / Q000235:genetics / Q000502:physiology
D017931:DNA Primers; D004279:DNA, Viral; D015247:Deoxyribonuclease HindIII