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RISS 인기검색어
- 검색키워드
- 저자 : ( Faysal Bin Hamid ) (검색결과 4 건)
- 무료
- 기관 내 무료
- 유료
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Cellular and viral determinants of retroviral nuclear entry
Hamid, Faysal Bin,Kim, Jinsun,Shin, Cha-Gyun Canadian Science Publishing 2016 Canadian journal of microbiology Vol.62 No.1
<P>Retroviruses must integrate their cDNA into the host genome to generate proviruses. Viral DNA-protein complexes interact with cellular proteins and produce pre-integration complexes, which carry the viral genome and cross the nuclear pore channel to enter the nucleus and integrate viral DNA into host chromosomal DNA. If the reverse transcripts fail to integrate, linear or circular DNA species such as 1- and 2-long terminal repeats are generated. Such complexes encounter numerous cellular proteins in the cytoplasm, which restrict viral infection and protect the nucleus. To overcome host cell defenses, the pathogens have evolved several evasion strategies. Viral proteins often contain nuclear localization signals, allowing entry into the nucleus. Among more than 1000 proteins identified as required for HIV infection by RNA interference screening, karyopherins, cleavage and polyadenylation specific factor 6, and nucleoporins have been predominantly studied. This review discusses current opinions about the synergistic relationship between the viral and cellular factors involved in nuclear import, with focus on the unveiled mysteries of the host-pathogen interaction, and highlights novel approaches to pinpoint therapeutic targets.</P>
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( Faysal Bin Hamid ),( Jinsun Kim ),( Cha-gyun Shin ) 한국미생물 · 생명공학회 2017 Journal of microbiology and biotechnology Vol.27 No.2
The foamy viruses are currently considered essential for development as vectors for gene delivery. Previous studies demonstrated that prototype foamy virus (PFV) can infect and replicate prevalently in a variety of cell types for its exclusive replication strategy. However, the virus-host interaction, especially PFV-transportin3 (TNPO3), is still poorly understood. In our investigation of the role of TNPO3 in PFV infection, we found lower virus production in TNPO3 knockdown (KD) cells compared with wild-type 293T cells. PCR analysis revealed that viral DNAs were mostly altered to circular forms: both 1-long terminal repeat (1-LTR) and 2-LTR in TNPO3 KD cells. We therefore suggest that TNPO3 is required for successful PFV replication, at least at/after the nuclear entry step of viral DNA. These findings highlight the obscure mysteries of PFV-host interaction and the requirement of TNPO3 for productive infection of PFV in 293T cells.
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Apoptotic events induced by prototype foamy virus infection
김진선,Faysal Bin Hamid,신차균 한국통합생물학회 2016 Animal cells and systems Vol.20 No.1
Foamy virus infection induces cytopathology in several cell types from different species. But the exact mechanism is still unknown. In this study, we have investigated the mechanism of cell death induced by prototype foamy virus (PFV) infection in baby hamster kidney (BHK 21) cell lines. PFV induces apoptosis by exhibiting morphological alterations such as chromatin condensation, blebbing, and nuclear fragmentation. In addition, PFV infection causes chromosomal DNA fragmentation, up-regulation of Bax, and activation of caspase-3, but not caspase-8. Up-regulation of Bax initiates the translocation of cytochrome-c from mitochondria to the cytoplasm, suggesting predominantly to the mitochondrial-mediated pathway. Blocking apoptosis using caspase inhibitors increased PFV-infected BHK 21 cell viability. Although blocking apoptosis resulted in reduced progeny release, maximal accumulation of PFV was found in apoptosis-blocked cells. This report provides the first experimental evidence of apoptosis induced by PFV infection, which will provide valuable insights for foamy viral pathology.
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Knockdown of the host cellular protein transportin 3 attenuates prototype foamy virus infection.
Ali, Md Khadem,Kim, Jinsun,Hamid, Faysal Bin,Shin, Cha-Gyun Japan Society for Bioscience, Biotechnology, and A 2015 Bioscience, Biotechnology, and Biochemistry Vol.79 No.6
<P>Transportin 3 (TNPO3) is a member of the importin-s superfamily proteins. Despite numerous studies, the exact molecular mechanism of TNPO3 in retroviral infection is still controversial. Here, we provide evidence for the role and mechanism of TNPO3 in the replication of prototype foamy virus (PFV). Our findings revealed that PFV infection was reduced 2-fold by knockdown (KD) of TNPO3. However, late stage of viral replication including transcription, translation, viral assembly, and release was not influenced. The differential cellular localization of PFV integrase (IN) in KD cells pinpointed a remarkable reduction of viral replication at the nuclear import step. We also found that TNPO3 interacted with PFV IN but not with Gag, suggesting that IN-TNPO3 interaction is important for nuclear import of PFV pre-integration complex. Our report enlightens the mechanism of PFV interaction with TNPO3 and support ongoing research on PFV as a promising safe vector for gene therapy.</P>
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