Internalization and trafficking mechanisms of coxsackievirus B3 in HeLa cells

Journal Article · Tue Mar 01 04:00:00 EST 2005 · Virology

DOI:https://doi.org/10.1016/j.virol.2004.12.010· OSTI ID:20637212

Chung, Sun-Ku ^[1]; Kim, Joo-Young ^[2]; Kim, In-Beom ^[3]; Park, Sang-Ick ^[2]; Paek, Kyung-Hee ^[4]; Nam, Jae-Hwan ^[2]

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1. Department of Biomedical Sciences, National Institute of Health, 5 Nokbun-dong, Eunpyung-gu, Seoul, 122-701 (Korea, Republic of) and Graduate School of Biotechnology (Korea, Republic of) University, Seoul, 136-701 (Korea, Republic of)
2. Department of Biomedical Sciences, National Institute of Health, 5 Nokbun-dong, Eunpyung-gu, Seoul, 122-701 (Korea, Republic of)
3. Department of Anatomy, College of Medicine, The Catholic University of Korea, Seoul, 137-701 (Korea, Republic of)
4. Graduate School of Biotechnology (Korea, Republic of) University, Seoul, 136-701 (Korea, Republic of)

Coxsackievirus B3 (CVB3) is nonenveloped and has a single-stranded positive-sense RNA genome. CVB3 induces myocarditis and ultimately dilated cardiomyopathy. Although there are mounting evidences of an interaction between CVB3 particles and the cellular receptors, coxsackievirus and adenovirus receptor (CAR) and decay-accelerating factor (DAF), very little is known about the mechanisms of internalization and trafficking. In the present study, we used the CVB3 H3 strain, which is CAR-dependent but DAF-independent Woodruff variant and found that during entry, CVB3 particles were colocalized in clathrin, after interacting primarily with CAR, which was not recycled to the plasma membrane. We also found that CVB3 internalization was dependent on the function of dynamin, a large GTPase that has an essential role in endocytosis. Heat-shock cognate protein, Hsc70, which acts as a chaperone in the release of coat proteins from clathrin-coated vesicles (CCV), played a role in CVB3 trafficking processes. Moreover, endosomal acidification was crucial for CVB3 endocytosis. Finally, CVB3 was colocalized in early endosome autoantigen 1 (EEA1) molecules, which are involved in endosome-endosome tethering and fusion. In conclusion, these data together indicate that CVB3 uses clathrin-mediated endocytosis and is transcytosed to early endosomes.

• OSTI ID: 20637212
• Journal Information: Virology, Journal Name: Virology Journal Issue: 1 Vol. 333; ISSN VIRLAX; ISSN 0042-6822
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
ACIDIFICATION
ADENOVIRUS
AUTOMOBILES
HEAT
PARTICLES
RECEPTORS
RNA