Virally coded noncapsid protein associated with bovine parvovirus infection

Lederman, Muriel; Patton, John T.; Stout, Ernest R.; Bates, Robert C.

doi:10.1128/jvi.49.2.315-318.1984

Cited by 45 publications

(18 citation statements)

References 21 publications

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“…Conserved motifs associated with rolling circle replication, helicase, and ATPase were identified within the NS protein. NP1 is a highly phosphorylated protein of currently undetermined function [38]; NP1 differed in length between species, ranging from 214 to 219 amino acids. Situated within the VP1-unique (VP1u) region, the phospholipase A2 motifs required for parvovirus infectivity were found in all 6 genomes, together with the calcium-binding loop and catalytic residues.…”

Section: Widespread Geographic Distribution Of Human Bocaviruses and mentioning

confidence: 99%

Human Bocaviruses Are Highly Diverse, Dispersed, Recombination Prone, and Prevalent in Enteric Infections

et al. 2010

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A new species of parvovirus tentatively named human bocavirus 4 (HBoV4) was genetically characterized. Among 641 feces samples from children and adults the most commonly detected bocaviruses species were HBoV2>HBoV3>HBoV4>HBoV1 with HBoV2 prevalence of 21% and 26% in Nigerian and Tunisian children. HBoV3 and HBoV4 species combined were found in 12/192 cases of non-polio acute flaccid paralysis (AFP) from Tunisia and Nigeria and 0/96 healthy Tunisian contacts (p=0.01). Evidence of extensive recombination at the NP1 and VP1 gene boundary between and within species was found. The multiple species and high degree of genetic diversity seen among the human bocaviruses found in feces relative to the highly homogeneous HBoV1 suggest that this world-wide distributed respiratory pathogen may have recently evolved from an enteric bocavirus, perhaps after acquiring an expanded tropism favoring the respiratory track. Elucidating the possible role of the newly identified enteric bocaviruses in human diseases including AFP and diarrhea will require further epidemiological studies.

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Section: Widespread Geographic Distribution Of Human Bocaviruses and mentioning

confidence: 99%

Human Bocaviruses Are Highly Diverse, Dispersed, Recombination Prone, and Prevalent in Enteric Infections

et al. 2010

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“…In MVM, two nonstructural polypeptides of 83 and 24 kDa were identified from the in vitro translation of 4.8-and 1.8-kilobase virusspecific RNA transcripts, respectively (8). Cell-free translation of bovine parvovirus-specific RNA revealed only a 28-kDa noncapsid polypeptide (12). 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).…”

mentioning

confidence: 99%

Identification and characterization of a porcine parvovirus nonstructural polypeptide

Molitor¹,

Joo²,

Collett³

1985

J Virol

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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.

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“…2B, treatment with IFN-α rapidly stimulated nuclear translocation of both STAT1 and STAT2, and this translocation was not affected in cells overexpressing NP1, demonstrating that NP1 has no effect on IFN-αinduced nuclear translocation of STAT1/2. Furthermore, similar to Bovine parvovirus (BPV), minute virus of canines (MVC), and HBoV Lederman et al, 1984;Sukhu et al, 2013), PBoV NP1 was localized in the nucleus (Fig. 2B).…”

Section: Np1 Does Not Prevent Stat1/stat2 Phosphorylation and Nuclearmentioning

confidence: 90%

Porcine bocavirus NP1 negatively regulates interferon signaling pathway by targeting the DNA-binding domain of IRF9

et al. 2015

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To subvert host antiviral immune responses, many viruses have evolved countermeasures to inhibit IFN signaling pathway. Porcine bocavirus (PBoV), a newly identified porcine parvovirus, has received attention because it shows clinically high co-infection prevalence with other pathogens in post-weaning multisystemic wasting syndrome (PWMS) and diarrheic piglets. In this study, we screened the structural and non-structural proteins encoded by PBoV and found that the non-structural protein NP1 significantly suppressed IFN-stimulated response element (ISRE) activity and subsequent IFN-stimulated gene (ISG) expression. However, NP1 affected neither the activation and translocation of STAT1/STAT2, nor the formation of the heterotrimeric transcription factor complex ISGF3 (STAT1/STAT2/IRF9). Detailed analysis demonstrated that PBoV NP1 blocked the ISGF3 DNA-binding activity by combining with the DNA-binding domain (DBD) of IRF9. In summary, these results indicate that PBoV NP1 interferes with type I IFN signaling pathway by blocking DNA binding of ISGF3 to attenuate innate immune responses.

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Virally coded noncapsid protein associated with bovine parvovirus infection

Cited by 45 publications

References 21 publications

Human Bocaviruses Are Highly Diverse, Dispersed, Recombination Prone, and Prevalent in Enteric Infections

Human Bocaviruses Are Highly Diverse, Dispersed, Recombination Prone, and Prevalent in Enteric Infections

Identification and characterization of a porcine parvovirus nonstructural polypeptide

Porcine bocavirus NP1 negatively regulates interferon signaling pathway by targeting the DNA-binding domain of IRF9

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