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Recombinant production of anti-HIV protein, griffithsin, by auto-induction in a fermentor culture.

Recombinant production of anti-HIV protein, griffithsin, by auto-induction in a fermentor culture. Research Abstract Details 

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  • Recombinant production of anti-HIV protein, griffithsin, by auto-induction in a fermentor culture. Abstract Text:

    barbara giomarelliBarbara Giomarelli,kathryn m schumacherKathryn M Schumacher,troy e taylorTroy E Taylor,raymond c sowderRaymond C Sowder,james l hartleyJames L Hartley,james b mcmahonJames B McMahon,toshiyuki moriToshiyuki Mori,

    Griffithsin (GRFT) is a novel anti-HIV protein isolated from the red alga Griffithia sp. The potent anti-viral activity of GRFT against both laboratory and primary isolates of HIV at picomolar concentrations makes this protein an attractive candidate microbicide to prevent sexual transmission of HIV. Here, we describe the recombinant production and purification of a biologically active hexa-histidine-tagged GRFT (His-GRFT) from Escherichia coli. To facilitate a large-scale production of recombinant His-GRFT, we tested different expression conditions to optimize the expression in the cytoplasm of E. coli to increase the overall production of soluble His-GRFT. Attempts to express His-GRFT in shake flask cultures resulted in a modest yield of soluble His-GRFT, with a large accumulation of the protein in inclusion bodies. The use of a fermenter and of a rich, auto-inducing medium allowed the total amount of His-GRFT per liter to be increased by about 45-fold, with approximately 70% of the protein expressed in the soluble fraction. N-terminal sequencing and MALDI-TOF analyses of the recombinant His-GRFT confirmed that the initial methionine residue was cleaved off. Recombinant His-GRFT showed equivalent activity with natural GRFT, both in respect to gp120-binding characteristics as well as anti-HIV activity. Size-exclusion chromatography analysis showed that both native GRFT and recombinant His-GRFT existed as homodimers in solution. The expression system described in this work provides a basis for the mass production of GRFT to allow further studies of the protein and investigation of therapeutic and preventive strategies against HIV.

    Recombinant production of anti-HIV protein, griffithsin, by auto-induction in a fermentor culture. Publishing Authors By Initials

    b giomarelliB Giomarelli,km schumacherKM Schumacher,te taylorTE Taylor,rc sowderRC Sowder,jl hartleyJL Hartley,jb mcmahonJB McMahon,t moriT Mori,

    For similar investigative techniques: clinical laboratory techniques: microbiological techniques: virus inactivation research abstracts see: investigative techniques: clinical laboratory techniques: microbiological techniques: virus inactivation research

    PUBMED ID PMID:

    MEDLINE DATE:

    Recombinant production of anti-HIV protein, griffithsin, by auto-induction in a fermentor culture. Journal Published:

    PUBLICATION TYPE: Research Support, N.I.H., Intr

    Journal: Protein expression and purification

    VOLUME: 47

    Page Numbers: 194-202

    Journal Abbreviation: Protein Expr. Purif.

    ISSN: 1046-5928

    DAY: 7

    MONTH: 11

    YEAR: 2005

    Recombinant production of anti-HIV protein, griffithsin, by auto-induction in a fermentor culture. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 9101496

    Recombinant production of anti-HIV protein, griffithsin, by auto-induction in a fermentor culture. Keywords Mesh Terms:

    KEYWORDS: Virus Inactivation

    MESH TERMS: pharmacology

    Chemical & Substance for Abstract: Recombinant production of anti-HIV protein, griffithsin, by auto-induction in a fermentor culture. Information

    Substance Name: griffithsin protein, Griffithsia

    Registry Number: 0

    Grant and Affiliation Information for Recombinant production of anti-HIV protein, griffithsin, by auto-induction in a fermentor culture.

    AFFILIATION: Molecular Targets Development Program, Center for Cancer Research, National Cancer Institute, NCI-Frederick, Frederick, MD 21702-1201, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NCI

    GRANT: N01-CO-12400

    ACRONYM: CO

    MEDLINETA: Protein Expr Purif

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    Number Hits: 0

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