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by
Yuan Lin |
Total Records (
3 ) for
Yuan Lin |
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De-Ming Yin
,
Fen Li
,
Xi-Jun Wang
,
Yuan Lin
,
Zeng-Zai Liu
,
Ning-Bo Xia
,
Xiao-Feng Sheng
,
Ting Wang
,
Yi Liu
and
Wei Liu
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Little information is available about prevalence of helminthes
in pigs in Hunan Province. In the present study, the prevalence of helminths
in adult pigs was investigated in Hunan Province, People’s
Republic of China between 2009 and 2012. A total of 690 pigs slaughtered in
local abattoirs from ten representative administrative regions in Hunan Province
were examined for the presence of helminths using traditional helminthological
approach. The worms were examined, counted and identified to species according
to existing keys and descriptions. A total of eight species of helminths were
found in pigs which represent three classes. The results of the present investigation
have important implications for the control of helminth infections in pigs in
Hunan Province, China. |
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Minghao Sun
,
Sandra M. Fuentes
,
Khalid Timani
,
Dengyun Sun
,
Chris Murphy
,
Yuan Lin
,
Avery August
,
Michael N. Teng
and
Biao He
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The order Mononegavirales (comprised of nonsegmented negative-stranded RNA viruses or NNSVs) contains many important pathogens. Parainfluenza virus 5 (PIV5), formerly known as simian virus 5, is a prototypical paramyxovirus and encodes a V protein, which has a cysteine-rich C terminus that is conserved among all paramyxoviruses. The V protein of PIV5, like that of many other paramyxoviruses, plays an important role in regulating viral RNA synthesis. In this work, we show that V interacts with Akt, a serine/threonine kinase, also known as protein kinase B. Both pharmacological inhibitors and small interfering RNA against Akt1 reduced PIV5 replication, indicating that Akt plays a critical role in PIV5 replication. Furthermore, treatment with Akt inhibitors also reduced the replication of several other paramyxoviruses, as well as vesicular stomatitis virus, the prototypical rhabdovirus, indicating that Akt may play a more universal role in NNSV replication. The phosphoproteins (P proteins) of NNSVs are essential cofactors for the viral RNA polymerase complex and require heavy phosphorylation for their activity. Inhibition of Akt activity reduced the level of P phosphorylation, suggesting that Akt is involved in regulating viral RNA synthesis. In addition, Akt1 phosphorylated a recombinant P protein of PIV5 purified from bacteria. The finding that Akt plays a critical role in replication of NNSV will lead to a better understanding of how these viruses replicate, as well as novel strategies to treat infectious diseases caused by NNSVs. |
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Khalid A. Timani
,
Dengyun Sun
,
Minghao Sun
,
Celia Keim
,
Yuan Lin
,
Phuong Tieu Schmitt
,
Anthony P. Schmitt
and
Biao He
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Parainfluenza virus 5 (PIV5) is a prototypical paramyxovirus. The V/P gene of PIV5 encodes two mRNA species through a process of pseudotemplated insertion of two G residues at a specific site during transcription, resulting in two viral proteins, V and P, whose N termini of 164 amino acid residues are identical. Previously it was reported that mutating six amino acid residues within this identical region results in a recombinant PIV5 (rPIV5-CPI–) that exhibits elevated viral protein expression and induces production of cytokines, such as beta interferon and interleukin 6. Because the six mutations correspond to the shared region of the V protein and the P protein, it is not clear whether the phenotypes associated with rPIV5-CPI– are due to mutations in the P protein and/or mutations in the V protein. To address this question, we used a minigenome system and recombinant viruses to study the effects of mutations on the functions of the P and V proteins. We found that the P protein with six amino acid residue changes (Pcpi–) was more efficient than wild-type P in facilitating replication of viral RNA, while the V protein with six amino acid residue changes (Vcpi–) still inhibits minigenome replication as does the wild-type V protein. These results indicate that elevated viral gene expression in rPIV5-CPI– virus-infected cells can be attributed to a P protein with an increased ability to facilitate viral RNA synthesis. Furthermore, we found that a single amino acid residue change at position 157 of the P protein from Ser (the residue in the wild-type P protein) to Phe (the residue in Pcpi–) is sufficient for elevated viral gene expression. Using mass spectrometry and 33P labeling, we found that residue S157 of the P protein is phosphorylated. Based on these results, we propose that phosphorylation of the P protein at residue 157 plays an important role in regulating viral RNA replication. |
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