한빛사논문
- 조회343
Hyunwook Lee1,7, Ruben Assaraf2,3,7, Suriyasri Subramanian4, Dan Goetschius4, Jan Bieri2, Nadia M. DiNunno4, Remo Leisi2, Carol M. Bator1, Susan L. Hafenstein1,5,6 & Carlos Ros2
1The Hormel Institute, University of Minnesota, Austin, MN, USA.
2Department of Chemistry, Biochemistry and Pharmaceutical Sciences, University of Bern, Bern, Switzerland.
3Graduate School for Cellular and Biomedical Sciences, Bern, Switzerland.
4The Pennsylvania State College of Medicine, Hershey, PA, USA.
5Department of Biochemistry, Biophysics and Molecular Biology, University of Minnesota, Minneapolis, MN, USA.
6Department of Infectious Diseases, Mayo Clinic, Rochester, MN, USA.
7These authors contributed equally: Hyunwook Lee, Ruben Assaraf.
Corresponding authors
Correspondence to Susan L. Hafenstein or Carlos Ros.
Abstract
The lack of a permissive cell culture system has limited high-resolution structures of parvovirus B19 (B19V) to virus-like particles (VLPs). In this study, we present the atomic resolution structure (2.2 Å) of authentic B19V purified from a patient blood sample. There are significant differences compared to non-infectious VLPs. Most strikingly, two host protease inhibitors (PIs), inter-alpha-trypsin inhibitor heavy chain 4 (ITIH4) and serpinA3, were identified in complex with the capsids in all patient samples tested. The ITIH4 binds specifically to the icosahedral fivefold axis and serpinA3 occupies the twofold axis. The protein-coated virions remain infectious, and the capsid-associated PIs retain activity; however, upon virion interaction with target cells, the PIs dissociate from the capsid prior to viral entry. Our finding of an infectious virion shielded by bound host serum proteins suggests an evolutionarily favored phenomenon to evade immune surveillance and escape host protease activity.
논문정보
- Research article
- 2024년 11월 (BRIC 등록일 2024-11-08)
- 국외 연구진
- 생명과학 > 구조생물 및 생물물리학
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