Báo cáo khoa học: "The interaction of hepatitis A virus (HAV) with soluble forms of its cellular receptor 1 (HAVCR1) share the physiological requirements of infectivity in cell culture"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: The interaction of hepatitis A virus (HAV) with soluble forms of its cellular receptor 1 (HAVCR1) share the physiological requirements of infectivity in cell culture | Virology Journal BioMed Central Research The interaction of hepatitis A virus HAV with soluble forms of its cellular receptor 1 HAVCR1 share the physiological requirements of infectivity in cell culture Erica Silberstein Krishnamurthy Konduru and Gerardo G Kaplan Open Access Address Laboratory of Hepatitis and Related Emerging Agents Center for Biologics Evaluation and Research Food and Drug Administration 8800 Rockville Pike Bethesda MD 20892 USA Email Erica Silberstein - Krishnamurthy Konduru - Gerardo G Kaplan - gk@ Corresponding author Published 27 October 2009 Virology Journal 2009 6 175 doi I743-422X-6-I75 Received 20 August 2009 Accepted 27 October 2009 This article is available from http content 6 1 175 2009 Silberstein et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background Hepatitis A virus HAV an atypical Picornaviridae that causes acute hepatitis in humans usurps the HAV cellular receptor 1 HAVCR1 to infect cells. HAVCR1 is a class 1 integral membrane glycoprotein that contains two extracellular domains a virus-binding immunoglobulin-like IgV domain and a mucin-like domain that extends the IgV from the cell membrane. Soluble forms of HAVCR1 bind alter and neutralize cell culture-adapted HAV which is attenuated for humans. However the requirements of the HAV-HAVCR1 interaction have not been fully characterized and it has not been determined whether HAVCR1 also serves as a receptor for wildtype wt HAV. Here we used HAV soluble receptor neutralization and alteration assays to study the requirements of the HAV-HAVCR1 interaction and to determine whether HAVCR1 is also a receptor for wt HAV. .

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