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      Pinning Down Viral Proteins: A New Prototype for Virus–Host Cell Interaction

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          Abstract

          Pin 1 is an enzyme that specifically catalyzes the cis–trans isomerization of phosphorylated serine/threonine-proline (pSer/Thr-Pro) motif in its substrate proteins. Recent studies demonstrate that stability of several viral proteins is regulated by phosphorylation-dependent prolyl-isomerization by a host factor Pin1. Pin1 is now positioned as an important modulator of the molecular crosstalk between virus and host cells and could be a unique target for anti-virus therapy. This new type of post-translational modification by Pin1 might be involved in the regulation of other viral proteins.

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          Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling.

          Tony Hunter (1995)
          Article 0 comments Cited 370 times – based on 0 reviews     Review now
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            The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease.

            Kun Lu, Xiao Zhou (2007)
            Protein phosphorylation regulates many cellular processes by causing changes in protein conformation. The prolyl isomerase PIN1 has been identified as a regulator of phosphorylation signalling that catalyses the conversion of specific phosphorylated motifs between the two completely distinct conformations in a subset of proteins. PIN1 regulates diverse cellular processes, including growth-signal responses, cell-cycle progression, cellular stress responses, neuronal function and immune responses. In line with the diverse physiological roles of PIN1, it has also been linked to several diseases that include cancer, Alzheimer's disease and asthma, and thus it might represent a novel therapeutic target.
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              Pin1 interacts with a specific serine-proline motif of hepatitis B virus X-protein to enhance hepatocarcinogenesis.

              Roberta WC Pang, Eric Tse, Victor Fan … (2007)
              The peptidyl prolyl isomerase Pin1 frequently is overexpressed in hepatocellular carcinoma (HCC). Hepatitis B virus (HBV) is the most common etiologic agent in HCC, and its encoded X-protein (HBx) is oncogenic and possesses a serine-proline motif that may bind Pin1. The role of Pin1 in hepatocarcinogenesis, particularly in HBV-related HCC, was investigated. Immunohistochemical staining was performed to evaluate the prevalence of Pin1 overexpression in HCCs of different etiologies. Glutathione S-transferase pull-down and co-immunoprecipitation experiments were used to validate the physical interaction between Pin1 and HBx. Reporter assay, cell proliferation assay, and xenotransplantation experiments were used to show the functional consequence and importance of Pin1-HBx interaction in hepatocarcinogenesis. We showed preferential Pin1 overexpression in HBV-related tumors and confirmed the interaction between Pin1 and HBx at the specific serine-proline motif. Pin1 overexpression increased the protein stability of HBx. Furthermore, HBx-mediated transactivation was enhanced by co-expression of Pin1. HepG2 expressing Pin1 and HBx showed a synergistic increase in cellular proliferation, as compared with cells expressing Pin1 or HBx alone. Furthermore, concomitant expression of Pin1 and HBx in the nontumorigenic human hepatocyte cell line MIHA led to a synergistic increase in tumor growth. Finally, in Hep3B cells with suppressed Pin1 expression, HBx-enhanced tumor growth in nude mice was abrogated. Pin1 binds HBx to enhance hepatocarcinogenesis in HBV-infected hepatocytes. The discovery of an interaction between Pin1 and HBx will further our understanding of the molecular pathogenic mechanism of HBV-related HCC in human beings.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Front Microbiol
                Journal ID (publisher-id): Front. Microbio.
                Title: Frontiers in Microbiology
                Publisher: Frontiers Research Foundation
                ISSN (Electronic): 1664-302X
                Publication date (Electronic preprint): 30 July 2010
                Publication date (Electronic): 09 September 2010
                Publication date Collection: 2010
                Volume: 1
                Electronic Location Identifier: 107
                Affiliations
                [1] 1simpleDepartment of Microbiology, Yokohama City University School of Medicine Yokohama, Kanagawa, Japan
                [2] 2simpleJapan Foundation for AIDS Prevention Tokyo, Japan
                Author notes

                Edited by: Hironori Sato, National Institute of Infectious Diseases, Japan

                Reviewed by: Masaru Yokoyama, National Institute of Infectious Diseases, Japan; Takao Masuda, Tokyo Medical and Dental University, Japan; Kazushi Motomura, National Institute of Infectious Diseases, Japan

                *Correspondence: Akihide Ryo, Department of Microbiology, Yokohama City University School of Medicine, 3-9 Fuku-ura, Kanazawa-ku, Yokohama, Kanagawa 236-0004, Japan. e-mail: aryo@ 123456yokohama-cu.ac.jp

                This article was submitted to Frontiers in Virology, a Specialty of Frontiers in Microbiology.

                Article
                DOI: 10.3389/fmicb.2010.00107
                PMC ID: 3125566
                PubMed ID: 21738521
                SO-VID: 13cd8049-2d36-4b52-a93c-9dc44d8f045f
                Copyright © Copyright© 2010 Kojima and Ryo.
                License:

                This is an open-access article subject to an exclusive license agreement between the authors and the Frontiers Research Foundation, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are credited.

                History
                Date received : 24 July 2010
                Date accepted : 09 August 2010
                Page count
                Figures: 1, Tables: 0, Equations: 0, References: 8, Pages: 2, Words: 1451
                Categories
                Subject: Microbiology
                Subject: Perspective Article

                ScienceOpen disciplines: Microbiology & Virology
                Keywords: pin1,protein stability,prolyl-isomerization,phosphorylation
                Data availability:
                ScienceOpen disciplines: Microbiology & Virology
                Keywords: pin1, protein stability, prolyl-isomerization, phosphorylation

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