مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Persian Verion

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

video

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

sound

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Persian Version

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

View:

999
مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Download:

0
مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Cites:

Information Journal Paper

Title

PRODUCTION OF THE PHOSPHOLIPASE D AND HEAT-SHOCK PROTEIN (HSP)-60 RECOMBINANT PROTEINS FROM CORYNEBACTERIUM PSEUDOTUBERCULOSIS

Pages

  121-127

Abstract

 BACKGROUND: Caseous lymphadenitis, caused by CORYNEBACTERIUM PSEUDOTUBERCULOSIS, is one of the most important diseases of sheep and goats, causing considerable losses for herd owners. PHOSPHOLIPASE D (PLD) is a potent exotoxin produced by C. pseudotuberculosis and it has been considered as the major virulence factor for this bacterium, possibly contributing to the spread of the bacteria from the initial site of infection to secondary sites within the host. Heat shock proteins (HSPs) are important candidates for the development of vaccines because they are usually able to promote both humoral and cellular immune responses in mammals.OBJECTIVES: The aim of this study was the CLONING and expression of the PLD and HSP60 genes of C. pseudotuberculosis, used subsequently to evaluate the protectivity of these recombinant proteins for vaccine development against this bacterium.METHODS: PLD and HSP60 genes were cloned into pMAL-c2X vector and recombinant plasmids construct was transformed to DH5 strain of E. coli. Expression of the proteins was shown by SDS-PAGE and accuracy of the cloned genes was confirmed by nucleotide sequence analysis.RESULTS: The transformed E. coli strain DH5 expressed PLD and HSP60 proteins effectively. The expressed fusion protein was found almost entirely in the soluble form.CONCLUSIONS: In the following studies the immunogenicity and protectivity of these recombinant proteins againstC. pseudotuberculosis infections can be assessed.

Cites

  • No record.
  • References

  • No record.
  • Cite

    APA: Copy

    BOROON, F., SEYFI ABAD SHAPOURI, M.R., GHORBANPOOR, M., GHARIBI, D., & ESMAEILZADEH, S.. (2017). PRODUCTION OF THE PHOSPHOLIPASE D AND HEAT-SHOCK PROTEIN (HSP)-60 RECOMBINANT PROTEINS FROM CORYNEBACTERIUM PSEUDOTUBERCULOSIS. JOURNAL OF VETERINARY RESEARCH, 72(1), 121-127. SID. https://sid.ir/paper/35351/en

    Vancouver: Copy

    BOROON F., SEYFI ABAD SHAPOURI M.R., GHORBANPOOR M., GHARIBI D., ESMAEILZADEH S.. PRODUCTION OF THE PHOSPHOLIPASE D AND HEAT-SHOCK PROTEIN (HSP)-60 RECOMBINANT PROTEINS FROM CORYNEBACTERIUM PSEUDOTUBERCULOSIS. JOURNAL OF VETERINARY RESEARCH[Internet]. 2017;72(1):121-127. Available from: https://sid.ir/paper/35351/en

    IEEE: Copy

    F. BOROON, M.R. SEYFI ABAD SHAPOURI, M. GHORBANPOOR, D. GHARIBI, and S. ESMAEILZADEH, “PRODUCTION OF THE PHOSPHOLIPASE D AND HEAT-SHOCK PROTEIN (HSP)-60 RECOMBINANT PROTEINS FROM CORYNEBACTERIUM PSEUDOTUBERCULOSIS,” JOURNAL OF VETERINARY RESEARCH, vol. 72, no. 1, pp. 121–127, 2017, [Online]. Available: https://sid.ir/paper/35351/en

    Related Journal Papers

    Related Seminar Papers

  • No record.
  • Related Plans

  • No record.
  • Recommended Workshops

  • No record.





  • Move to top
    telegram sharing button
    whatsapp sharing button
    linkedin sharing button
    twitter sharing button
    email sharing button
    email sharing button
    email sharing button
    sharethis sharing button