%0 Journal Article
	%A Yan Ren and  Fei Guo and  Jun Qiao and  Shengwei Hu and  Hui Zhang and  Yuanzhi Wang and  Pengyan Wang and  Jinliang Sheng and  Xinli Gu and  Xiaojun Liu and  Chuangfu Chen
	%D 2013
	%J International Journal of Biotechnology and Bioengineering
	%B World Academy of Science, Engineering and Technology
	%I Open Science Index 75, 2013
	%T Identification of Binding Proteins That Interact with BVDV E2 Protein in Bovine Trophoblast Cell
	%U https://publications.waset.org/pdf/7100
	%V 75
	%X Bovine viral diarrhea virus (BVDV) can cause lifelong
persistent infection. One reason for the phenomena is attributed to
BVDV infection to placenta tissue. However the mechanisms that
BVDV invades into placenta tissue remain unclear. To clarify the
molecular mechanisms, we investigated the possible means that
BVDV entered into bovine trophoblast cells (TPC). Yeast two-hybrid
system was used to identify proteins extracted from TPC, which
interact with BVDV envelope glycoprotein E2. A PGbkt7-E2 yeast
expression vector and TPC cDNA library were constructed. Through
two rounds of screening, three positive clones were identified.
Sequencing analysis indicated that all the three positive clones
encoded the same protein clathrin. Physical interaction between
clathrin and BVDV E2 protein was further confirmed by
coimmunoprecipitation experiments. This result suggested that the
clathrin might play a critical role in the process of BVDV entry into
placenta tissue and might be a novel antiviral target for preventing
BVDV infection.
	%P 239 - 242