Erratum to 'Endocytosis of Integrin-Binding Human Picornaviruses'
| العنوان: | Erratum to 'Endocytosis of Integrin-Binding Human Picornaviruses' |
|---|---|
| المؤلفون: | Petri Susi, Pirjo Merilahti, Satu Koskinen, Outi Heikkilä, Eveliina Karelehto |
| المصدر: | Advances in Virology Advances in Virology, Vol 2013 (2013) |
| بيانات النشر: | Hindawi Publishing Corporation, 2013. |
| سنة النشر: | 2013 |
| مصطلحات موضوعية: | biology, Endosome, media_common.quotation_subject, Integrin, Endocytosis, Microbiology, Virology, QR1-502, Cell biology, ESCRT complex, Infectious Diseases, MHC class I, Immunology, biology.protein, Small GTPase, Erratum, Internalization, Integrin binding, media_common |
| الوصف: | 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. Heikkila, 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. |
| اللغة: | English |
| تدمد: | 1687-8647 1687-8639 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5883558f915817357c4713076041c61Test http://europepmc.org/articles/PMC3638652Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....e5883558f915817357c4713076041c61 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 16878647 16878639 |
|---|