Crystal Structures of Plk1 Polo-Box Domain Bound to the Human Papillomavirus Minor Capsid Protein L2-Derived Peptide.


Journal

Journal of microbiology (Seoul, Korea)
ISSN: 1976-3794
Titre abrégé: J Microbiol
Pays: Korea (South)
ID NLM: 9703165

Informations de publication

Date de publication:
Aug 2023
Historique:
received: 09 06 2023
accepted: 09 08 2023
revised: 25 07 2023
medline: 10 10 2023
pubmed: 9 9 2023
entrez: 8 9 2023
Statut: ppublish

Résumé

Human papillomaviruses (HPVs) can increase the proliferation of infected cells during HPV-driven abnormalities, such as cervical cancer or benign warts. To date, more than 200 HPV genotypes have been identified, most of which are classified into three major genera: Alphapapillomavirus, Betapapillomavirus, and Gammapapillomavirus. HPV genomes commonly encode two structural (L1 and L2) and seven functional (E1, E2, E4-E7, and E8) proteins. L2, the minor structural protein of HPVs, not only serves as a viral capsid component but also interacts with various human proteins during viral infection. A recent report revealed that L2 of HPV16 recruits polo-like kinase 1 (Plk1), a master regulator of eukaryotic mitosis and cell cycle progression, for the delivery of viral DNA to mitotic chromatin during HPV16 infection. In this study, we verified the direct and potent interactions between the polo-box domain (PBD) of Plk1 and PBD-binding motif (S-S-pT-P)-containing phosphopeptides derived from L2 of HPV16/HPV18 (high-risk alphapapillomaviruses), HPV5b (low-risk betapapillomavirus), and HPV4 (low-risk gammapapillomavirus). Subsequent structural determination of the Plk1 PBD bound to the HPV18 or HPV4 L2-derived phosphopeptide demonstrated that they interact with each other in a canonical manner, in which electrostatic interactions and hydrogen bonds play key roles in sustaining the complex. Therefore, our structural and biochemical data imply that Plk1 is a broad binding target of L2 of various HPV genotypes belonging to the Alpha-, Beta-, and Gammapapillomavirus genera.

Identifiants

pubmed: 37684534
doi: 10.1007/s12275-023-00071-3
pii: 10.1007/s12275-023-00071-3
doi:

Substances chimiques

Capsid Proteins 0
Phosphopeptides 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

755-764

Subventions

Organisme : Ministry of Science and ICT, South Korea
ID : 2019M3E5D6063955
Organisme : Ministry of Science and ICT, South Korea
ID : CRC22021-700
Organisme : Ministry of Science and ICT, South Korea
ID : KGM9952314

Informations de copyright

© 2023. The Author(s), under exclusive licence to Microbiological Society of Korea.

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Auteurs

Sujin Jung (S)

Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, 34141, Republic of Korea.
Department of Biochemistry, Chungnam National University, Daejeon, 34134, Republic of Korea.

Hye Seon Lee (HS)

Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, 34141, Republic of Korea.

Ho-Chul Shin (HC)

Critical Diseases Diagnostics Convergence Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, 34141, Republic of Korea.

Joon Sig Choi (JS)

Department of Biochemistry, Chungnam National University, Daejeon, 34134, Republic of Korea.

Seung Jun Kim (SJ)

Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, 34141, Republic of Korea. ksj@kribb.re.kr.
Critical Diseases Diagnostics Convergence Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, 34141, Republic of Korea. ksj@kribb.re.kr.

Bonsu Ku (B)

Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, 34141, Republic of Korea. bku@kribb.re.kr.

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