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- 검색키워드
- 저자 : Md. Khadem Ali (검색결과 4 건)
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Md. Khadem Ali,Md. Alamgir Hossain,신차균 한국유전학회 2013 Genes & Genomics Vol.35 No.4
Transportin 3 (TNPO3 or TRN-SR2) is a key host cellular factor involved in the early steps of several lentiviral replications. In the present study, we cloned the TNPO3 gene from CV-1 cells of African green monkey (AGM) using a homologue based cloning technology,analyzed the sequence, and evaluated the cellular expression of the proteins by western blotting and immunostaining assays. DNA sequencing of TNPO3 showed homologies of 99 % with human, rhesus monkey, chimpanzee,and baboon; the predicted protein sequence differed in only one amino acid (leucine in place of methionine). The deduced sequence revealed that AGM is phylogenetically related to human, chimpanzee, rhesus monkey, orangutan and baboon rather than bovine, rate and mouse. Western blot analysis demonstrated immunoreactive proteins in both the cytoplasmic and nuclear fractions. A similar expression pattern was observed in human and baby hamster cells. The specific detection of TNPO3 was also confirmed in the cytoplasm and nucleus by immunostaining. The present findings conclusively demonstrate that AGM-TNPO3 is genetically and physiologically almost identical with that of humans and could be a good candidate for HIV and AGM research as well as an ideal system for a TNPO3 vaccine trial.
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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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Md. Alamgir Hossain,Md. Khadem Ali,신차균 한국분자세포생물학회 2014 Molecules and cells Vol.37 No.2
We identified four basic amino acid residues as nuclear localization signals (NLS) in the C-terminal domain of the prototype foamy viral (PFV) integrase (IN) protein that were essential for viral replication. We constructed seven point mutants in the C-terminal domain by changing the lysine and arginine at residues 305, 308, 313, 315, 318, 324, and 329 to threonine or proline, respectively, to identify residues conferring NLS activity. Our results showed that mu-tation of these residues had no effect on expression assembly, release of viral particles, or in vitro recombinant IN enzymatic activity. However, mutations at residues 305 (R → T), 313(R → T), 315(R → P), and 329(R → T) lead to the production of defective viral particles with loss of infectivity, whereas non-defective mutations at residues 308(R → T), 318(K → T), and 324(K → T) did not show any adverse effects on subsequent production or release of viral particles. Sub-cellular fractionation and immunostaining for viral protein PFV-IN and PFV-Gag localization revealed predominant cytoplasmic localization of PFV-IN in defective mutants, whereas cytoplasmic and nuclear localiza-tion of PFV-IN was observed in wild type and non-defective mutants. However sub-cellular localization of PFV-Gag re-sulted in predominant nuclear localization and less pre-sence in the cytop-lasm of the wild type and non-defective mutants. But defective mutants showed only nuclear localization of Gag. Therefore, we postulate that four basic arginine residues at 305, 313, 315 and 329 confer the karyoplilic properties of PFV-IN and are essential for successful viral integration and replication.
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Hossain, Md. Alamgir,Ali, Md. Khadem,Shin, Cha-Gyun Korean Society for Molecular and Cellular Biology 2014 Molecules and cells Vol.37 No.2
We identified four basic amino acid residues as nuclear localization signals (NLS) in the C-terminal domain of the prototype foamy viral (PFV) integrase (IN) protein that were essential for viral replication. We constructed seven point mutants in the C-terminal domain by changing the lysine and arginine at residues 305, 308, 313, 315, 318, 324, and 329 to threonine or proline, respectively, to identify residues conferring NLS activity. Our results showed that mutation of these residues had no effect on expression assembly, release of viral particles, or in vitro recombinant IN enzymatic activity. However, mutations at residues 305 (R ${\rightarrow}$ T), 313(R ${\rightarrow}$ T), 315(R ${\rightarrow}$ P), and 329(R ${\rightarrow}$ T) lead to the production of defective viral particles with loss of infectivity, whereas non-defective mutations at residues 308(R ${\rightarrow}$ T), 318(K ${\rightarrow}$ T), and 324(K ${\rightarrow}$ T) did not show any adverse effects on subsequent production or release of viral particles. Sub-cellular fractionation and immunostaining for viral protein PFV-IN and PFV-Gag localization revealed predominant cytoplasmic localization of PFV-IN in defective mutants, whereas cytoplasmic and nuclear localization of PFV-IN was observed in wild type and non-defective mutants. However sub-cellular localization of PFV-Gag resulted in predominant nuclear localization and less presence in the cytoplasm of the wild type and non-defective mutants. But defective mutants showed only nuclear localization of Gag. Therefore, we postulate that four basic arginine residues at 305, 313, 315 and 329 confer the karyoplilic properties of PFV-IN and are essential for successful viral integration and replication.
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