Advances in Virology

Volume 2013 (2013), Article ID 412909, 1 page

http://dx.doi.org/10.1155/2013/412909

Erratum

Erratum to “Endocytosis of Integrin-Binding Human Picornaviruses”

Pirjo Merilahti,1,2 Satu Koskinen,¹ Outi Heikkilä,1,2 Eveliina Karelehto,1,3 and Petri Susi1,2

¹Department of Virology, University of Turku, Kiinamyllynkatu 13, 20520 Turku, Finland

²Degree Program in Biotechnology and Food Technology, Turku University of Applied Sciences, Lemminkäisenkatu 30, 20520 Turku, Finland

³Joint Biotechnology Laboratory, University of Turku, Tykistökatu 6a, 20520 Turku, Finland

Received 27 February 2013; Accepted 7 March 2013

Copyright © 2013 Pirjo Merilahti et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Due to unfortunate errors at the proof-reading stage, there are several misplaced references. A list of correct references in specified sentences is provided here as follows.

Page 3: binding of E-1 to integrin α2β1 does not induce uncoating but instead may lead to the stabilization of capsid suggesting that viral RNA is released during endocytosis and not on plasma membrane .

Page 3: this was based on the virus accumulation in caveolin-1-positive endosomes in SAOS cells overexpressing integrin α2β1 . However, at the same time and using another cell model, CV-1, the same authors demonstrated that majority of E-1 do not colocalize with caveolin-1 on the plasma membrane . This observation was based on parallel comparisons to SV40, which is known to use caveolar route at least in some cell lines .

Page 4: dominant-negative caveolin-3 has been shown to block E-1 infection .

Page 4: which are localized in early endosomes and function in MVB formation .

Page 4: the recent finding that ESCRT complex recruits caveolin-1 into maturing intralumenal vesicles may explain why E-1 and caveolin-1 are found in similar structures early in infection .

Page 5: we recently showed that CV-A9 internalization is dependent on 2-microglobulin .

Page 5: Arf6 (ADP-ribosylation factor 6) is a small GTPase, which has multiple roles in the regulation of membrane traffic and other cellular functions, but it was only recently when it was linked to virus endocytosis .

Page 5: and this may explain why it remains highly pathogenic .

Page 5: which is evidently in contradiction with the suggestion that HPeV-1 is endocytosed via clathrin-mediated pathway . On the other hand, MHC I (with β2M) has been linked to internalization of β1-integrins, but previously not shown to be involved in HPeV-1 infection .

Page 9: the data in reference should be as follows: O. Heikkilä, E. Karelehto, P. Merilahti et al., “HSPA5 protein (GRP78) and b2-microglobulin mediate internalization and entry of coxsackievirus A9 via a novel Arf6-dependent entry pathway in human epithelial colon adenocarcinoma cells,” Submitted.