Earticle

초록

영어

Influenza virus hemagglutinin (HA) is expressed as a precursor protein, HA0, and then proteolytically cleaved to produce two disulfide-linked polypeptide chains, HA1 and HA2. The HA2 protein segment, an influenza virus glycoprotein, contains two membrane-interacting hydrophobic peptide sequences: an N-terminal "fusion peptide" (residues 1-22), which
interacts with the target membrane, and a C-terminal transmembrane domain (residues 186-221) that passes through the viral membrane. This study aims to develop biodegradable microparticles containing both HA1 and truncated HA2 proteins for vaccination with enhanced biosafety. The HA2 ectodomain (residues 23-185) truncated with two membraneinteracting
sequences was expressed in Escherichia coli. This segment of HA2 contains changes in three rare Arg codons (Arg-123, Arg-124, and Arg-127) and the mutation of Cys-137, which forms a disulfide bond with HA1 residue 14, to Ser. The full-length HA1 polypeptide segment was
expressed separately in Escherichia coli with mutation of Cys-14, which forms a disulfide bond with HA2 residue 137, to Ser. Both purified HA1 and truncated HA2 segments were microencapsulated in poly(D,L-lacticco-glycolic acid) (PLGA) using a W/O/W double emulsion technique. Antigen release from microspheres was determined in vitro using a hemagglutinin-specific ELISA.

키워드

저자

• Chang Sup KIM [ Division of Applied Chemistry & Biotechnology, Hanbat National University, Daejeon, 305-719. ]
• Yong JANG [ Division of Applied Chemistry & Biotechnology, Hanbat National University, Daejeon, 305-719. ]
• Sang Hern KIM [ Division of Applied Chemistry & Biotechnology, Hanbat National University, Daejeon, 305-719. ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576