首页 | 本学科首页   官方微博 | 高级检索  
     


Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport
Authors:M J Gething  K McCammon  J Sambrook
Affiliation:1. Discipline of Medical Biochemistry, College of Medicine and Public Health, Flinders University, Adelaide, South Australia, Australia;2. Discipline of Human Physiology, College of Medicine and Public Health, Flinders University, Adelaide, South Australia, Australia;3. The HPB and Liver Transplant Unit, Flinders Medical Centre and College of Medicine and Public Health, Flinders University, Adelaide, South Australia, Australia;4. Department of Surgery, Isala, Zwolle, The Netherlands;1. Institute of Experimental Physiology (IFISE-CONICET), Suipacha 570, 2000 Rosario, Argentina;2. University of Connecticut, School of Pharmacy, Department of Pharmaceutical Sciences, Storrs, CT, USA;3. Institute of Pharmacological Investigations (ININFA-CONICET), University of Buenos Aires, Buenos Aires, Argentina;4. Department of Clinical Pharmacology and Pharmacoepidemiology, University of Heidelberg, Heidelberg, Germany;1. Library of Marine Samples, Korea Institute of Ocean Science & Technology, Geoje 53201, Republic of Korea;2. Marine Ecosystem and Biological Research Center, Korea Institute of Ocean Science & Technology, Busan 49111, Republic of Korea;3. South Sea Research Center, Korea Institute of Ocean Science & Technology, Geoje 53201, Republic of Korea;4. Ballast Water Center, Korea Institute of Ocean Science & Technology, Geoje 53201, Republic of Korea;5. Korea Institute of Coastal Ecology, Inc., #801~3, IT 302, Ssangyong Technopark III, Gyeonggi-Do, 14449, Republic of Korea
Abstract:The hemagglutinin of influenza virus is synthesized as a monomeric subunit that is cotranslationally translocated across the membrane of the rough endoplasmic reticulum. We show that folding and assembly of hemagglutinin monomers into trimeric structures takes approximately 7-10 min and is completed before the protein leaves the endoplasmic reticulum. Mutants of hemagglutinin that fail to be transported from the endoplasmic reticulum are blocked at different stages of the folding pathway. Unfolded molecules of hemagglutinin are associated with a cellular protein of 77 kd that has been shown previously to bind to IgG heavy chain in the endoplasmic reticulum of certain myelomas. We discuss why assembly of native structures is required for transport of proteins through the exocytotic pathway.
Keywords:
本文献已被 ScienceDirect 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号