Characterization of hepatitis A virus structural proteins |
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| Authors: | V Gauss-Müller F Lottspeich F Deinhardt |
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| Affiliation: | 1. Max von Pettenkofer Institute for Hygiene and Medical Microbiology, University of Munich, Pellenkoferstrasse 9a D-8000 Munich 2, Germany;2. Gene Center, University of Munich, D-8033 Martinsried bei Munich, West Germany;1. Key Laboratory of Marine Drugs of Ministry of Education, Shandong Provincial Key Laboratory of Glycoscience and Glycotechnology, School of Medicine and Pharmacy, Ocean University of China, Qingdao, 266003, China;2. Laboratory for Marine Drugs and Bioproducts, Pilot National Laboratory for Marine Science and Technology (Qingdao), Qingdao, 266237, China;1. Department of Radiochemistry and Environmental Chemistry, Institute of Chemical Sciences, Faculty of Chemistry, Maria Curie-Sklodowska University in Lublin, Maria Curie-Sklodowska Sq. 3, 20-031, Lublin, Poland;2. Institute of Agrophysics, Polish Academy of Sciences, Doswiadczalna 4, 20-290, Lublin, Poland;1. Research Center, College of Computer and Information Sciences, Princess Nourah bint Abdulrahman University, Riyadh, Saudi Arabia;2. College of Computer and Information Sciences, Information Technology Department, King Saud University, Riyadh, Saudi Arabia;3. College of Computer and Information Sciences, Information Systems Department, King Saud University, Riyadh, Saudi Arabia;4. Research Chair in Healthcare Innovation, Information Systems Department, College of Computer and Information Sciences, King Saud University, Riyadh, Saudi Arabia |
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| Abstract: | HAV particles isolated from infected cells banded at buoyant densities of 1.42, 1.32, and 1.20 g/ml, and distinctive protein patterns were established by gel electrophoresis and reverse phase high performance liquid chromatography. The relatively higher amounts of p30 in particles with lower buoyant densities suggest that this protein is VP0 and is part of the immature picornavirion. The protein elution profiles obtained by HPLC were virtually identical for all the HAV strains examined but differed from those of other picornaviruses. The N-terminal amino acid sequence of VP1 and VP2 was determined and aligned to the nucleotide sequence. Sequencing VP0 and VP3 was not possible, probably because the amino termini are blocked. VP1, VP3, and VP0 induced specific antibodies in rabbits. |
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