Autor: |
Chervyakova OV; Research Institute for Biological Safety Problems, RK ME&S - Science Committee, Gvardeiskiy 080409, Kazakhstan. ovch@mail.ru., Zaitsev VL; Research Institute for Biological Safety Problems, RK ME&S - Science Committee, Gvardeiskiy 080409, Kazakhstan. biosafety@biosafety.kz., Iskakov BK; M. A. Aitkhozhin's Institute of Molecular Biology and Biochemistry, RK ME&S - Science Committee, Almaty 050012, Kazakhstan. bulat.isakakov@mail.ru., Tailakova ET; Research Institute for Biological Safety Problems, RK ME&S - Science Committee, Gvardeiskiy 080409, Kazakhstan. tailakova_86@mail.ru., Strochkov VM; Research Institute for Biological Safety Problems, RK ME&S - Science Committee, Gvardeiskiy 080409, Kazakhstan. vstrochkov@biosafety.kz., Sultankulova KT; Research Institute for Biological Safety Problems, RK ME&S - Science Committee, Gvardeiskiy 080409, Kazakhstan. sultankul70@mail.ru., Sandybayev NT; Research Institute for Biological Safety Problems, RK ME&S - Science Committee, Gvardeiskiy 080409, Kazakhstan. nurlan.s@mail.ru., Stanbekova GE; M. A. Aitkhozhin's Institute of Molecular Biology and Biochemistry, RK ME&S - Science Committee, Almaty 050012, Kazakhstan. gulshanst@yahoo.com., Beisenov DK; M. A. Aitkhozhin's Institute of Molecular Biology and Biochemistry, RK ME&S - Science Committee, Almaty 050012, Kazakhstan. daniyar.b@mail.ru., Abduraimov YO; Research Institute for Biological Safety Problems, RK ME&S - Science Committee, Gvardeiskiy 080409, Kazakhstan. yergali.a@gmail.com., Mambetaliyev M; Research Institute for Biological Safety Problems, RK ME&S - Science Committee, Gvardeiskiy 080409, Kazakhstan. murat@biosafety.kz., Sansyzbay AR; Research Institute for Biological Safety Problems, RK ME&S - Science Committee, Gvardeiskiy 080409, Kazakhstan. sansyzbai-ar@biosafety.kz., Kovalskaya NY; United States Department of Agriculture, Agricultural Research Service, Molecular Plant Pathology Laboratory, Beltsville, MD 20705, USA. natalia.kovalksaya@ars.usda.gov., Nemchinov LG; United States Department of Agriculture, Agricultural Research Service, Molecular Plant Pathology Laboratory, Beltsville, MD 20705, USA. lev.nemchinov@ars.usda.gov., Hammond RW; United States Department of Agriculture, Agricultural Research Service, Molecular Plant Pathology Laboratory, Beltsville, MD 20705, USA. rose.hammond@ars.usda.gov. |
Abstrakt: |
The aim of this work was to evaluate the immunogenicity and neutralizing activity of sheep pox virus (SPPV; genus Capripoxvirus, family Poxviridae) structural proteins as candidate subunit vaccines to control sheep pox disease. SPPV structural proteins were identified by sequence homology with proteins of vaccinia virus (VACV) strain Copenhagen. Four SPPV proteins (SPPV-ORF 060, SPPV-ORF 095, SPPV-ORF 117, and SPPV-ORF 122), orthologs of immunodominant L1, A4, A27, and A33 VACV proteins, respectively, were produced in Escherichia coli. Western blot analysis revealed the antigenic and immunogenic properties of SPPV-060, SPPV-095, SPPV-117 and SPPV-122 proteins when injected with adjuvant into experimental rabbits. Virus-neutralizing activity against SPPV in lamb kidney cell culture was detected for polyclonal antisera raised to SPPV-060, SPPV-117, and SPPV-122 proteins. To our knowledge, this is the first report demonstrating the virus-neutralizing activities of antisera raised to SPPV-060, SPPV-117, and SPPV-122 proteins. |