Evaluation of skimmed milk flocculation method for virus recovery from tomatoes

Melgaço, Fabiana Gil; Corrêa, Adriana Abreu; Ganime, Ana Carolina; Brandão, Marcelo Luiz Lima; Medeiros, Valéria de Mello; Rosas, Carla de Oliveira; Lopes, Silvia Maria dos Reis; Miagostovich, Marize Pereira

doi:10.1016/j.bjm.2018.04.014

Cited by 13 publications

(5 citation statements)

References 41 publications

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“…For the GI.1 VLPs, the A/B dimers have a convex S domain conformation, whereas the C/C dimers have a flat S domain conformation (8). The conformational differences within these dimers likely facilitates the curvature of the virus particle to form a closed shell, such features are commonly seen in other T=3 icosahedral viruses (26). Interestingly, smaller norovirus VLPs (~25 nm in diameter) that are assumed to have a T=1 icosahedral symmetry have also been reported (22,27); however to date, structures of these smaller VLPs have not been published.…”

Section: Introductionmentioning

confidence: 94%

Heterologous expression of human norovirus GII.4 VP1 leads to assembly of T=4 virus-like particles

et al. 2019

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Human noroviruses are a leading cause of acute gastroenteritis, yet there are still no vaccines or antivirals available. Expression of the norovirus capsid protein (VP1) in insect cells typically results in the formation of virus-like particles (VLPs) that are morphologically and antigenically comparable to native virions. Previous structural analysis of norovirus VLPs showed that the capsid has a T=3 icosahedral symmetry and is composed of 180 copies of VP1 that are folded into three quasi-equivalent subunits (A, B, and C). In this study, we determined the cryo-EM VLP structures of two GII.4 variants, termed CHDC-1974 and NSW-2012. Surprisingly, we found that greater than 95% of these GII.4 VLPs were larger than virions and 3D reconstruction showed that these VLPs exhibited T=4 icosahedral symmetry. We found that the T=4 VLPs showed several structural differences to the T=3 VLPs. The T=4 particles assemble from 240 copies of VP1 that adopt four quasi-equivalent conformations (A, B, C, and D) that form two distinct dimers, A/B and C/D. The T=4 protruding domains were elevated ~21-Å off the capsid shell, which was ~7-Å more than the previously studied GII.10 T=3 VLPs. A small cavity and flap-like structure at the icosahedral twofold axis disrupted the contiguous T=4 shell, a consequence of the Dsubunit S-domains having smaller contact interfaces with neighboring dimers.Overall, our findings that old and new GII.4 VP1 sequences assemble T=4 VLPs might have implications for the design of potential future vaccines.

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Section: Introductionmentioning

confidence: 94%

Heterologous expression of human norovirus GII.4 VP1 leads to assembly of T=4 virus-like particles

et al. 2019

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“…For the GI.1 VLPs, the A/B dimers have a bent S domain conformation, whereas the C/C dimers have flat S domain conformation (7). The conformational differences within these dimers likely facilitates the curvature of the virus particle to form a closed shell, which is commonly seen in other T=3 icosahedral viruses (14). Interestingly, smaller norovirus VLPs (~25 nm in diameter) that are assumed to have a T=1 icosahedral symmetry were also reported (15, 16); however the structure of these smaller VLPs has not yet been determined.…”

Section: Introductionmentioning

confidence: 82%

Novel Structural Features of Human Norovirus Capsid

Devant

Hofhaus

Hansman

2019

Preprint

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16Human noroviruses are a major cause of gastroenteritis, yet there are still no vaccines 17 or antivirals available. Nevertheless, a number of vaccine candidates that are currently 18 in clinical trials are composed of norovirus virus-like particles (VLPs). These VLPs 19 are recognized as morphologically and antigenically similar to norovirus virions. An 20 X-ray crystal structure of the prototype (GI.1) VLPs showed that the norovirus capsid 21 has a T=3 icosahedral symmetry and is composed of 180 copies of the major capsid 22 protein (VP1) that folds into three quasi-equivalent subunits (A, B, and C). In this 23 study, we determined the cryo-EM structure of VLPs for two GII.4 noroviruses that 24were detected in 1974 and 2012. We showed that these VLPs had a T=4 symmetry 25 and were composed of 240 copies of VP1. The VP1 on the T=4 VLPs adapted four 26 quasi-equivalent subunits (termed A, B, C, and D), which formed two distinct dimers 27 (A/B and C/D). We found that the T=4 protruding domain was elevated ~21 Å off the 28 capsid shell, which was ~7 Å more than the previously determined for the T=3 GII.10 29 norovirus. Another interesting feature of the T=4 VLPs was a small cavity and flap-30 like structure located at the twofold axis. This structural feature was associated with 31 the shell domain (D subunit) and disrupted the contiguous shell. Altogether, we 32 showed that the T=4 VLPs had a number of structural similarities and differences 33 with other noroviruses, but how these structural changes associate with norovirus 34 virions could be important for vaccine studies. 35 65 tolerated, highly immunogenic, and appeared to be safe, since they did not comprise 66 of live or attenuated virus. However, limitations of the current vaccine formulations 67 included mild norovirus like-symptoms, restricted long-term immunity, and limited 68 cross-protection (5, 6). 69 70 Structural analysis of GI.1 VLPs reveals that VP1 is separated into two distinct 71 domains: a shell domain (S domain) that encloses the RNA and a protruding domain 72 Journal of physics. Condensed matter : an Institute of Physics journal 421 30:064006.

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“…The LVC method followed by a second concentration step was compared to the SMF method, which has been extensively used for virus concentration from diverse types of environmental samples (Assis et al, 2017;Calgua et al, 2013aCalgua et al, , 2013bCalgua et al, 2008;Gonzales-Gustavson et al, 2017a, 2017bMelgaço et al, 2018).…”

Section: Comparison Of the Lvc Methods + Secondary Concentration To S...mentioning

confidence: 99%

Evaluation of a Virus Concentration Method Based on Ultrafiltration and Wet Foam Elution for Studying Viruses from Large-Volume Water Samples

Forés¹,

Rusiñol²,

Itarte³

et al. 2021

SSRN Journal

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Evaluation of skimmed milk flocculation method for virus recovery from tomatoes

Cited by 13 publications

References 41 publications

Heterologous expression of human norovirus GII.4 VP1 leads to assembly of T=4 virus-like particles

Heterologous expression of human norovirus GII.4 VP1 leads to assembly of T=4 virus-like particles

Novel Structural Features of Human Norovirus Capsid

Evaluation of a Virus Concentration Method Based on Ultrafiltration and Wet Foam Elution for Studying Viruses from Large-Volume Water Samples

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