- Structural and biochemical analysis of the PTPN4 PDZ domain bound to the C-terminal tail of the human papillomavirus E6 oncoprotein
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Hye Seon Lee , Hye-Yeoung Yun , Eun-Woo Lee , Ho-Chul Shin , Seung Jun Kim , Bonsu Ku
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J. Microbiol. 2022;60(4):395-401. Published online January 28, 2022
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DOI: https://doi.org/10.1007/s12275-022-1606-1
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High-risk genotypes of human papillomaviruses (HPVs) are
directly implicated in various abnormalities associated with
cellular hyperproliferation, including cervical cancer. E6 is one
of two oncoproteins encoded in the HPV genome, which recruits
diverse PSD-95/Dlg/ZO-1 (PDZ) domain-containing
human proteins through its C-terminal PDZ-binding motif
(PBM) to be degraded by means of the proteasome pathway.
Among the three PDZ domain-containing protein tyrosine
phosphatases, protein tyrosine phosphatase non-receptor type
3 (PTPN3) and PTPN13 were identified to be recognized by
HPV E6 in a PBM-dependent manner. However, whether
HPV E6 associates with PTPN4, which also has a PDZ domain
and functions as an apoptosis regulator, remains undetermined.
Herein, we present structural and biochemical evidence
demonstrating the direct interaction between the PBM
of HPV16 E6 and the PDZ domain of human PTPN4 for the
first time. X-ray crystallographic structure determination and
binding measurements using isothermal titration calorimetry
demonstrated that hydrophobic interactions in which Leu158
of HPV16 E6 plays a key role and a network of intermolecular
hydrogen bonds sustain the complex formation between
PTPN4 PDZ and the PBM of HPV16 E6. In addition, it was
verified that the corresponding motifs from several other highrisk
HPV genotypes, including HPV18, HPV31, HPV33, and
HPV45, bind to PTPN4 PDZ with comparable affinities, suggesting
that PTPN4 is a common target of various pathogenic
HPV genotypes.
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Citations
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Sujin Jung, Dahwan Lim, Joon Sig Choi, Ho-Chul Shin, Seung Jun Kim, Bonsu Ku
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- Genetic Diversity of Chromosomal Metallo-β-Lactamase Genes in Clinical Isolates of Elizabethkingia meningoseptica from Korea
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Jong Hwa Yum , Eun Young Lee , Sung-Ho Hur , Seok Hoon Jeong , Hyukmin Lee , Dongeun Yong , Yunsop Chong , Eun-Woo Lee , Patrice Nordmann , Kyungwon Lee
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J. Microbiol. 2010;48(3):358-364. Published online June 23, 2010
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DOI: https://doi.org/10.1007/s12275-010-9308-5
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836
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This study was performed to characterize the chromosomal metallo-β-lactamases (MBLs) of Elizabethkingia meningoseptica isolated from Korea and to propose a clustering method of BlaB and GOB MBLs based on their amino acid similarities. Chromosomal MBL genes were amplified by PCR from 31 clinical isolates of E.
meningoseptica. These PCR products were then cloned into a vector and electrotransformed into E. coli DH5α. Nucleotide sequencing was performed by the dideoxy chain termination method using PCR products or cloned DNA fragments. Antimicrobial susceptibilities were determined by the agar dilution method. PCR
experiments showed that all 31 E. meningoseptica isolates contained both the blaB and the blaGOB genes. DNA sequence analysis revealed that E. meningoseptica isolates possessed seven types of blaB gene, including five novel variants (blaB-9 to blaB-13) and 11 types of blaGOB gene, including 10 novel variants (blaGOB-8 to blaGOB-17). The most common combination of MBL was BlaB-12 plus GOB-17 (n=19). Minimum inhibitory concentrations of imipenem and meropenem for the electrotransformants harboring novel BlaB and GOB MBLs were two- or four-fold higher than those for the recipient E. coli DH5α. BlaB and GOB MBLs were
grouped in three and six clusters including fifteen novel variants, respectively, based on amino acid similarities.
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Citations
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