Transcription and translation in the autonomous parvovirus KRV

Mitra, Ruchira; Wali, Tonu; Valdez, Vincent; Fabisch, P; Salzman, Lois Ann

doi:10.1016/0042-6822(83)90207-6

Cited by 10 publications

(11 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Parvovirus nonstructural proteins of lower masses (24 to 28 kDa) have also been described (8,12,15). In vitro translation of MVM-specific RNA revealed, in addition to an 83-kDa NS-1 polypeptide (antigenically related to PPV NS-1), a 24-kDa nonstructural polypeptide, .…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Identification and characterization of a porcine parvovirus nonstructural polypeptide

Molitor¹,

Joo²,

Collett³

1985

J Virol

View full text Add to dashboard Cite

Sera from porcine parvovirus (PPV)-infected swine fetuses immunoprecipitated and 84to 86-kilodalton polypeptide in addition to the A and B virion structural proteins. This polypeptide, designated NS-1, was present in PPV-infected cell lysates but not in purified virions. Partial proteolysis mapping revealed that NS-1 was not related to the A and B viral structural proteins. All three proteins in infected cells were phosphorylated at serine residues, and NS-1 also contained phosphothreonine. From pulse-labeling experiments with either 32p, or [35S]methionine, NS-1 was found to first appear 5 to 7 h postinfection, whereas the viral structural polypeptides were first synthesized 9 to 11 h postinfection. Pulse-chase experiments revealed that NS-1 initially appeared as an 84-kilodalton protein and was subsequently structurally modified to forms of slower electrophoretic mobilities. The time of appearance of NS-1 after virus infection coincided with the initiation of viral DNA synthesis, suggesting that this polypeptide (and the modified forms thereof) may be involved in PPV replication.

show abstract

Section: Discussionmentioning

confidence: 99%

“…Virus-specific antiserum was used in the identification of two forms of a nonstructural protein (84 and 94 kDa) from H-1 parvovirus-infected cells (18). Viral noncapsid polypeptides have also been described in Kilham rat virus-infected (15), rabbit parvovirus-infected (13), and Aleutian disease virus-infected (2) cells.…”

mentioning

confidence: 99%

Identification and characterization of a porcine parvovirus nonstructural polypeptide

Molitor¹,

Joo²,

Collett³

1985

J Virol

View full text Add to dashboard Cite

show abstract

“…Among rodent parvoviruses, such as the minute virus of mice (MVM), H-1, HER and RV, a serologic crossreactivity has been shown by the immunofluorescent antibody (IFA) test, but not by the HI, neutralization and complement fixation tests [5,12] . The cross-reactivity of rodent parvoviruses could be due to virus-coded, non-structural protein which was recognized for several autonomous parvoviruses [3,14] . In the present study, the crossreactivity to other rodent parvoviruses would be eliminated in ELISA, since ELISA antigen was prepared from purified viral particles which did not contain non-structural protein.…”

Section: Discussionmentioning

confidence: 99%

The Advantage of Enzyme-linked Immunosorbent Assay (ELISA) as a Method of Microbiological Monitoring for Rat Virus (RV)

Izumi

Fukazawa

Sugiyama

et al. 1991

Experimental Animals

View full text Add to dashboard Cite

An enzyme-linked immunosorbent assay (ELISA) was tested to detect antibodies against rat virus (RV). The purified ELISA antigens were prepared from rat embryonic cells infected with RV-13 (prototype strain) and UT-2 (Japanese isolate), respectively. Western blotting analysis confirmed that both of these antigens had three structural polypeptides (81K, 61K, and 59K). Eleven laboratory and wild rat colonies in Japan were tested for rat virus contamination, serologically. No significant differences in the sero-positive ratio and the distributions of ELISA titers were demonstrated in the ELISA, using antigens from RV-13 and UT-2. ELISA was more sensitive and specific for detecting antibodies against RV from rat serum rather than hemagglutination inhibition (HI) test. This study also confirmed that the RV contaminated widely in colonies of laboratory and wild rats in Japan, and suggested that RV would have to be checked during the microbiological monitoring of laboratory rats.

show abstract

“…Virus-coded non-structural proteins have been recognized for several of the autonomous parvoviruses and are probably a common feature of the genus (Bloom et al, 1982;Cotmore et al, 1983;Lederman et al, 1984;Mitra et al, 1983;Matsunaga & Matsuno, 1983;Molitor et al, 1985;Paradiso, 1984;Pintel et al, 1983). It is possible that for at least some of the autonomous parvoviruses, common antigens are associated mainly with non-structural proteins.…”

Section: Antigenic Relationships Among Autonomous Parvovirusesmentioning

confidence: 99%

Antigenic Relationships among Autonomous Parvoviruses

Mengeling

Paul

Bunn

et al. 1986

Journal of General Virology

View full text Add to dashboard Cite

SUMMARYThe antigenic relatedness of minute virus of mice (MVM), Kilham rat virus (KR), H-1 virus (H-1), haemorrhagic encephalopathy of rats virus (HER), porcine parvovirus (PPV), canine parvovirus (CPV), feline panleukopenia virus (FPV), goose parvovirus (GPV) and bovine parvovirus (BPV) was studied by immunofluorescence microscopy (FA) and by serum neutralization (SN). An antigenically related group comprising MVM, KR, HER, PPV, CPV and FPV was recognized by FA and most reactions within the group were reciprocal. Antigenic relatedness was less evident when the same viruses and antisera were tested by SN. Only CPV and FPV were closely and reciprocally related. Other cross-reactions by SN were quantitatively minor and included neutralization of CPV and FPV by pig anti-PPV serum and neutralization of H-1 and HER by rat anti-KR serum. Neither FA nor SN revealed any antigenic relationship of BPV and GPV either with each other or with any of the other viruses tested.

show abstract

Transcription and translation in the autonomous parvovirus KRV

Cited by 10 publications

References 26 publications

Identification and characterization of a porcine parvovirus nonstructural polypeptide

Identification and characterization of a porcine parvovirus nonstructural polypeptide

The Advantage of Enzyme-linked Immunosorbent Assay (ELISA) as a Method of Microbiological Monitoring for Rat Virus (RV)

Antigenic Relationships among Autonomous Parvoviruses

Contact Info

Product

Resources

About