AV
Advances in Virology
1687-8647
1687-8639
Hindawi Publishing Corporation
412909
10.1155/2013/412909
412909
Erratum
Erratum to “Endocytosis of Integrin-Binding Human Picornaviruses”
Merilahti
Pirjo
1, 2
Koskinen
Satu
1
Heikkilä
Outi
1, 2
Karelehto
Eveliina
1, 3
Susi
Petri
1, 2
1
Department of Virology
University of Turku
Kiinamyllynkatu 13
20520 Turku
Finland
utu.fi
2
Degree Program in Biotechnology and Food Technology
Turku University of Applied Sciences
Lemminkäisenkatu 30
20520 Turku
Finland
tuas.fi
3
Joint Biotechnology Laboratory
University of Turku
Tykistökatu 6a
20520 Turku
Finland
utu.fi
2013
3
4
2013
2013
27
02
2013
07
03
2013
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 [54,60].
Page 3: this was based on the virus accumulation in caveolin-1-positive endosomes in SAOS cells overexpressing integrin α2β1 [60,66]. 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 [67]. This observation was based on parallel comparisons to SV40, which is known to use caveolar route at least in some cell lines [62].
Page 4: dominant-negative caveolin-3 has been shown to block E-1 infection [68].
Page 4: which are localized in early endosomes and function in MVB formation [69].
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 [66,69].
Page 5: we recently showed that CV-A9 internalization is dependent on β2-microglobulin [72].
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 [72].
Page 5: and this may explain why it remains highly pathogenic [75,76].
Page 5: which is evidently in contradiction with the suggestion that HPeV-1 is endocytosed via clathrin-mediated pathway [105]. 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 [105].
Page 9: the data in reference [83] 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.