High-Yield Expression and Purification of Recombinant σB Protein of Avian Reovirus (ARV) in Prokaryotic System

نویسندگان

  • Sanjeevna K. Minhas
  • Nitin M. Kamble
  • J. M. Kataria
  • Madhan Mohan
  • Sohini Dey
چکیده

Avian reovirus (ARV) infection is a ubiquitous disease of poultry, affecting mostly broiler breeds. Pathogenic effects of ARV such as arthritis and tenosynovitis are attributed to significant economic losses to poultry industry. ARV is classified under genus Orthoreovirus of family Reoviridae (Van Regenmortel et al., 2000). The genome of ARV encodes at least ten structural proteins (λA, λB, λC, μA, μB, μBC, μBN, σC, σA and σB) and four non-structural proteins (μNS, P10, P17 and σNS) (Benavente and Martínez-Costas, 2007). Among these proteins, S3 gene-encoded σB is a major outer capsid protein of ARV, functioning in the induction of cell fusion and viral pathogenesis (Ni and Ramig, 1993). ARV σB protein is structurally similar to the σB protein of Duck reoviruses and Mammalian reoviruses (Vakharia et al., 1996; Yin et al., 1997) and share functional similarity with them. The σB protein is also known to induce group-specific International Journal of Current Microbiology and Applied Sciences ISSN: 2319-7706 Volume 6 Number 9 (2017) pp. 434-441 Journal homepage: http://www.ijcmas.com

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Antigenic Analysis of Monoclonal Antibodies against Different Epitopes of σB Protein of Avian Reovirus

BACKGROUND Avian reovirus (ARV) causes arthritis, tenosynovitis, runting-stunting syndrome (RSS), malabsorption syndrome (MAS) and immunosuppression in chickens. σB is one of the major structural proteins of ARV, which is able to induce group-specific antibodies against the virus. METHODS AND RESULTS The present study described the identification of two linear B-cell epitopes in ARV σB throug...

متن کامل

Prokaryotic expression, purification and immunogenicity analysis of CpsD protein from Streptococcus iniae

Streptococcus iniae is a major cause of serious bacterial infections in both fish and human beings. Capsular polysaccharide (CPS) of S. iniae is vital to evade phagocytic clearance of the host and serves as an important protective antigen of S. iniae infection in aquatic animals. The CpsD gene was determined to be highly conservative in capsule polysaccharide operon. Prokaryotic expression of t...

متن کامل

Prokaryotic expression, purification and immunogenicity analysis of CpsD protein from Streptococcus iniae

Streptococcus iniae is a major cause of serious bacterial infections in both fish and human beings. Capsular polysaccharide (CPS) of S. iniae is vital to evade phagocytic clearance of the host and serves as an important protective antigen of S. iniae infection in aquatic animals. The CpsD gene was determined to be highly conservative in capsule polysaccharide operon. Prokaryotic expression of t...

متن کامل

Cloning, Expression and Purification of Creatininase From Pseudomonas Pseudoalkaligene KF707 in E. coli.

Creatinine amidohydrolase(EC 3.5.2.10) catalyzes the reversible conversion of creatinine to creatine. Creatininase in combination with other enzymes is used for detection of creatinine in serum and urine which is of significant value for detection of renal, muscular and thyroid functions. The aim of this study was to produce recombinant creatininase enzyme in E.coli expression system to use it ...

متن کامل

Prokaryotic Expression, Purification, and Polyclonal Antibody Production of a Truncated Recombinant Rabies Virus L Protein

Background: Rabies virus (RABV) is a deadly neurotropic virus that causes the disease of rabies in humans and animals. L protein is one of the large structural protein of rabies virus, which displays multiple enzymatic activities, and is required for viral transcription and replication. Objectives: A truncated L protein of Rabies virus is being cloned, expressed and purified to produce relevant...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2017