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Special Issue "Phage Display in Virus Research"

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A special issue of Viruses (ISSN 1999-4915).

Deadline for manuscript submissions: closed (30 April 2014)

Special Issue Editor

Guest Editor
Prof. Dr. Dr. Xiaofeng Ren

Department of Preventive Veterinary Medicine, College of Veterinary Medicine, Northeast Agricultural University, 59 Mucai Street, Xiangfang District, Harbin 150030, China

Special Issue Information

Dear Colleagues,

Increasing evidence indicate that phage display technology, a powerful molecular tool, has been effectively employed in virus research. Successful examples included HIV, hepatitis B virus, hepatitis c virus, avian influenza virus and coronavirus etc. This special issue will overview achieved results in virus research by utilizing of phage display. Various phage display systems such as T4, T7 or M13 phages and different target proteins such as viral antigens or cellular components can be analyzed or reviewed in the context of virology. It will emphasize, but not limit to diagnostic application and mechanism investigation aspects by identifying potential peptide ligands to viral related targets or virus epitope/mimotope domains. Characterizations of phage displayed peptides such as immunological potential or structural predication are also welcome. Review on applied advances and basic research of phage display in virology field are particularly appreciated.

Prof. Dr. Dr. Xiaofeng Ren
Guest Editor

Submission

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Viruses is an international peer-reviewed Open Access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1500 CHF (Swiss Francs).

Keywords

  • phage display
  • viruses
  • peptide ligands
  • diagnosis
  • infection

Published Papers (2 papers)

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Research

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Open AccessArticle Generation and Characterization of a Novel Recombinant Antibody against LMP1-TES1 of Epstein-Barr Virus Isolated by Phage Display
Viruses 2013, 5(4), 1131-1142; doi:10.3390/v5041131
Received: 6 February 2013 / Revised: 11 April 2013 / Accepted: 15 April 2013 / Published: 22 April 2013
Cited by 4 | PDF Full-text (417 KB) | HTML Full-text | XML Full-text
Abstract
Latent Membrane Protein 1 (LMP1) is a primary target for controlling tumorigenesis in Epstein-Barr virus related malignancies; in this study, we aimed to develop a specific antibody against the TES1 domain of the oncogenic LMP1. We screened a full human naïve Fab [...] Read more.
Latent Membrane Protein 1 (LMP1) is a primary target for controlling tumorigenesis in Epstein-Barr virus related malignancies; in this study, we aimed to develop a specific antibody against the TES1 domain of the oncogenic LMP1. We screened a full human naïve Fab phage library against TES1 peptide, which consisted of C terminal-activating regions proximal 44 amino acids. After three rounds of panning, enrichment and testing by phage ELISA and further analyzed by DNA sequencing, we selected a phage clone with the highest affinity to LMP1-TES1 and designated it as htesFab. The positive clone was expressed in Escherichia coli and the purified htesFab was characterized for its binding specificity and affinity to LMP1. ELISA, immunofluorescence and FACS analysis confirmed that htesFab could recognize LMP1 TES1 both in vitro and in LMP1 expressing HNE2-LMP1 cells. Furthermore, MTT assay showed that htesFab inhibited the proliferation of HNE2-LMP1 cells in a dose-dependent manner. In summary, this study reported the isolation and characterization of human Fab, which specifically targets the C terminal region/TES1 of LMP1, and has potential to be developed as novel tool for the diagnosis and therapy of Epstein-Barr virus related carcinoma Full article
(This article belongs to the Special Issue Phage Display in Virus Research)

Review

Jump to: Research

Open AccessReview Oligopeptide M13 Phage Display in Pathogen Research
Viruses 2013, 5(10), 2531-2545; doi:10.3390/v5102531
Received: 17 September 2013 / Revised: 8 October 2013 / Accepted: 9 October 2013 / Published: 16 October 2013
Cited by 7 | PDF Full-text (243 KB) | HTML Full-text | XML Full-text
Abstract
Phage display has become an established, widely used method for selection of peptides, antibodies or alternative scaffolds. The use of phage display for the selection of antigens from genomic or cDNA libraries of pathogens which is an alternative to the classical way [...] Read more.
Phage display has become an established, widely used method for selection of peptides, antibodies or alternative scaffolds. The use of phage display for the selection of antigens from genomic or cDNA libraries of pathogens which is an alternative to the classical way of identifying immunogenic proteins is not well-known. In recent years several new applications for oligopeptide phage display in disease related fields have been developed which has led to the identification of various new antigens. These novel identified immunogenic proteins provide new insights into host pathogen interactions and can be used for the development of new diagnostic tests and vaccines. In this review we focus on the M13 oligopeptide phage display system for pathogen research but will also give examples for lambda phage display and for applications in other disease related fields. In addition, a detailed technical work flow for the identification of immunogenic oligopeptides using the pHORF system is given. The described identification of immunogenic proteins of pathogens using oligopeptide phage display can be linked to antibody phage display resulting in a vaccine pipeline. Full article
(This article belongs to the Special Issue Phage Display in Virus Research)

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