Determination by peptide mapping of the unique polypeptides in sendai virions and infected cells

Lamb, Robert A.; Choppin, Purnell W.

doi:10.1016/0042-6822(78)90263-5

Cited by 72 publications

(39 citation statements)

References 21 publications

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“…4). This map is also the same as the peptide map of actin published by Lamb & Choppin (1978), confirming that this protein is actin. We were unable to control the relative amount of actin in the virus preparation, but the proportion of this protein present can be regarded as a measure of the purity of a particular preparation, because a higher content of actin was correlated with increased amounts of other cellular contaminants (e.g.…”

Section: Actin Is Present In I B Vsupporting

confidence: 70%

Polypeptides of Infectious Bronchitis Virus. I. Polypeptides of the Virion

Lomniczi

Morser

1981

Journal of General Virology

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Section: Actin Is Present In I B Vsupporting

confidence: 70%

Polypeptides of Infectious Bronchitis Virus. I. Polypeptides of the Virion

Lomniczi

Morser

1981

Journal of General Virology

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“…C protein is considered to be a nonstructural protein (15). Therefore, it was unexpected that our 10 ts mutants from the mutagenized stocks represented only three complementation groups, and furthermore that four (ts-5, -9, -10, -201) or possibly five mutants (ts-25 in addition) out of our 10 mutants are members of one complementation group, the HANA group.…”

Section: Discussionmentioning

confidence: 99%

Isolation and Characterization of Temperature‐Sensitive Mutants of Sendai Virus

Adachi

Kanda

Shibuta

1980

Microbiology and Immunology

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Sixteen temperature-sensitive mutants of Sendai virus were isolated from mutagenized stocks (10 mutants, designated numerically) and persistently infected cultures (6 mutants, designated alphabetically) .Based on complementation tests, virion-associated activities, thermal inactivation, and viral RNA and hemadsorbing antigen synthesis as well as virion production in chick lung embryo cells at nonpermissive temperature , these mutants were divided into seven groups as follows.i) HANA group mutants (ts-5, -9, -10, -201), defective in hemagglutininneuraminidase protein, complementation group I. ii) F group mutants (ts-18, -108), defective in hemolytic and cell-fusing activity , complementation group II . iii) Ts-43, defective in RNA polymerase activity, complementation group III . iv) Ts-23, defective in RNA polymerase activity, interfered with the other mutants in complementation tests. v) Ts-25, defective in the incorporation of hemagglutinin-neuraminidase protein into the virion at the stage of virus assembly. vi) Ts-110, belongs to F group mutants on one hand, but is considered to carry another undetermined defect. vii) C group (carrier culture-borne group) mutants (ts-a, -b, -c, -d, -e, -f), defective lesion not yet determined and belong to neither complementation group I nor II . Assignment of mutants in groups iv), v), vi), and vii) to complementation groups could not be achieved .Ten temperature-sensitive (ts) mutants of Sendai virus have been isolated from mutagenized virus stocks (22) and one from a persistently infected culture (10) . The former were divided into seven complementation groups (22). Among these 11 ts mutants, however, only a few were characterized in terms of defective protein (9,11,21,23,24). We isolated 16 ts mutants from mutagenized virus stocks as well as persistently infected cultures, i.e., carrier cultures, and analyzed these mutants genetically, biochemically and biologically.

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“…This is more than the seven so far identified in Sendai virus (Lamb & Choppin, 1978) and morbilliviruses (Rims & Martin, I979), but further studies are required to establish whether these are all primary gene products.…”

Section: S H O R T C O M M U N I C a T I O N Smentioning

confidence: 99%

“…At present it is not possible to assign functions to the 45K polypeptide and the smaller 23K and I7K polypeptides. The 23K polypeptide may be analogous to the C protein found in Sendai virus-infected cells (Lamb & Choppin, 1978) and we have identified a very small polypeptide in measles and canine distemper virus-infected cells (Rims & Martin, 1979). The appearance of the C and S polypeptides in infected cells labelled for short periods with zsS-methionine in the presence of the proteolytic enzyme inhibitor L-tosylamide-2-phenylethyl-chloromethyl-ketone (TPCK; Fig.…”

Section: S H O R T C O M M U N I C a T I O N Smentioning

confidence: 99%