Alcohol consumption, drinking patterns, and cognitive performance in young adults : A cross-sectional and longitudinal analysis
Hendriks, Henk ; Rest, Ondine van de; Snippe, Almar ; Kieboom, Jasper ; Hogenelst, Koen - \ 2020
Nutrients 12 (2020)1. - ISSN 2072-6643
Alcohol consumption - Cognitive performance - Young adult
Long-term alcohol abuse is associated with poorer cognitive performance. However, the associations between light and moderate drinking and cognitive performance are less clear. We assessed this association via cross-sectional and longitudinal analyses in a sample of 702 Dutch students. At baseline, alcohol consumption was assessed using questionnaires and ecological momentary assessment (EMA) across four weeks (‘Wave 1’). Subsequently, cognitive performance, including memory, planning, and reasoning, was assessed at home using six standard cognition tests presented through an online platform. A year later, 436 students completed the four weeks of EMA and online cognitive testing (‘Wave 2’). In both waves, there was no association between alcohol consumption and cognitive performance. Further, alcohol consumption during Wave 1 was not related to cognitive performance at Wave 2. In addition, EMA-data-based drinking patterns, which varied widely between persons but were relatively consistent over time within persons, were also not associated with cognitive performance. Post-hoc analyses of cognitive performance revealed higher within-person variance scores (from Wave 1 to Wave 2) than between-person variance scores (both Wave 1 and Wave 2). In conclusion, no association was observed between alcohol consumption and cognitive performance in a large Dutch student sample. However, the online cognitive tests performed at home may not have been sensitive enough to pick up differences in cognitive performance associated with alcohol consumption.
The cytoplasmic domain of tomato spotted witl virus Gn glycoprotein is required for Golgi localisation and interaction with Gc
Snippe, M. ; Smeenk, L. ; Goldbach, R.W. ; Kormelink, R.J.M. - \ 2007
Virology 363 (2007)2. - ISSN 0042-6822 - p. 272 - 279.
intracellular-transport - hantaan virus - retention - g1 - signal - coexpression - trafficking - expression - complex - cells
Envelopment of tomato spotted wilt virus nucleocapsids occurs at the Golgi stacks of infected cells. This is also the place where the two membrane glycoproteins Gn and Gc accumulate upon coexpression. The required Golgi retention signal has previously been demonstrated to reside within Gn. Using a series of truncated Gn proteins, the Golgi retention signal was mapped to a stretch of 10 amino acids on this protein's cytoplasmic tail, 20 residues downstream the transmembrane domain. Studies on the intracellular distribution of chimeric Gc proteins in which the cytoplasmic tail and/or transmembrane domain were exchanged by those from Gn, demonstrated the additional requirement of the Gn transmembrane domain for Golgi targeting. Truncated Gn constructs lacking the C-terminal 20 amino acids but still localising to the Golgi were no longer able to redirect Gc, suggesting the requirement of this domain for interaction with Gc.
Tomato spotted wilt virus Gc and N proteins interact in vivo
Snippe, M. ; Borst, J.W. ; Goldbach, R.W. ; Kormelink, R.J.M. - \ 2007
Virology 357 (2007)2. - ISSN 0042-6822 - p. 115 - 123.
nucleocapsid protein - fluorescence microscopy - mammalian-cells - matrix protein - living cells - fever virus - membrane - glycoproteins - localization - microtubules
Tomato spotted wilt virus (TSWV) virions consist of a nucleocapsid core surrounded by a membrane containing glycoproteins Gn and Gc. To unravel the protein interactions involved in the membrane acquisition of RNPs, TSWV nucleocapsid protein (N), Gn and Gc were expressed and analyzed in BHK21 cells. Upon coexpression of Gn, Gc and N, a partial colocalization of N with both glycoproteins was observed in the Golgi region. In contrast, upon coexpression of Gc and N in the absence of Gn, both proteins colocalized to a distinct non-Golgi perinuclear region. Using FLIM and FRET, interaction was demonstrated between N and Gc, but not between N and Gn, and was only observed in the region where both proteins accumulated. The genuine character of N¿Gc interaction was confirmed by its presence in purified virus and RNP preparations. The results are discussed in view of TSWV particle assembly taking place at the Golgi complex
|TSWV particle assembly: studying protein targeting and interaction between the structural proteins in vivo
Snippe, M. ; Kormelink, R.J.M. ; Goldbach, R.W. - \ 2006
In: Suppression and Circumvention of Host Defence by Plant Viruses, 1 - 5 July, 2006, Helsinki, Finland. - Helsinki : - p. 53 - 53.
Tomato spotted wilt virus particle assembly : studying the role of the structural proteins in vivo
Snippe, M. - \ 2006
Wageningen University. Promotor(en): R.W. Goldbach, co-promotor(en): Richard Kormelink. - [S.l. ] : S.n. - ISBN 9789085043263 - 128
solanum lycopersicum - tomaten - tomatenbronsvlekkenvirus - tospovirus - viruseiwitten - virale regulatoire eiwitten - glycoproteïnen - fluorescentiemicroscopie - genexpressieanalyse - solanum lycopersicum - tomatoes - tomato spotted wilt virus - tospovirus - viral proteins - viral regulatory proteins - glycoproteins - fluorescence microscopy - genomics
Members of the Bunyaviridae have spherical, enveloped virus particles that acquire their lipid membrane at the Golgi complex. For the animal-infecting bunyaviruses, virus assembly involves budding of ribonucleoprotein particles (RNPs) into vacuolised lumen of the Golgi complex, after which the enveloped particles are secreted. The maturation of tomato spotted wilt virus (TSWV), a bunyavirus infecting plants, is different in that virions acquire their membrane by wrapping of a Golgi stack around RNPs after which the enveloped particles eventually accumulate in large vesicles in the plant cell. TSWV also multiplies in its insect vector thrips, and here particles are secreted from salivary gland cells into the gland ducts. The latter seems a logic requirement to allow virus passage to healthy host plants.To further study the process of TSWV particle assembly, the interactions between the structural N, Gn and Gc proteins in mature virus particles, as well as their intracellular behaviour invivo havebeen the main target of this Ph. D. thesis.After an introductory chapter on bunyavirus particle assembly (chapter 1), the protein composition of purified TSWV RNPs and enveloped particles was studied in chapter 2.In enveloped virus preparations, the three major structural proteins, i.e. the nucleocapsid protein (N) and the two envelope glycoproteins Gn andGc, were detected in monomeric as well as oligomeric forms. GlycoproteinGcbut not Gn was observed tightly bound to RNPs, suggesting Gc is involved in RNP envelopment. Analysis of cytoplasmic RNPs and mature virus particles for other viral proteins revealed, surprisingly, the presence of the so-called nonstructural protein NSs. Whereas mature virus particles contained only traces of NSs, RNP preparations clearly contained larger amounts of this protein, which could be related to an earlier reported difference in transcriptional/replicational activity between both.To study the process of virus assembly in more detail, fluorescence microscopy methods were employed for the in vivo detection of protein interactions, rendering information concerning the intracellular localisation simultaneously (chapter 3). For this a system was set up in mammalian cells and as a first protein to be studied the cytosolic N protein was selected. This protein was already known to form homo-oligomeric structures in vitro. Using fusions of N with either yellow or cyan fluorescent protein (YFP and CFP, respectively), pairs were created to function as a donor (CFP) and acceptor (YFP) fluorophore for fluorescence resonance energy transfer (FRET). Using acceptor photobleaching and fluorescence lifetime imaging microscopy (FLIM) to measure FRET, N was observed to form homodimers and -multimers throughout the cytoplasm before eventually accumulating in a non-Golgi, perinuclear region ona microtubuli- and actin-dependent manner.In a similar way, potential in vivo interactions between N and the viral glycoproteins were investigated (chapter 4). While no interaction between N and Gn was observed, these studies demonstrated interaction between N andGc, inagreementwith the earlier observation (chapter 2) that some Gc remains tightly bound to purified RNPs. The interactions between N andGclocalised to the non-Golgi perinuclear area, similar to transiently expressed N. These data provided further support for the idea that interactions between N andGcare involved in envelopment of the viral RNPs. While studying the possible formation of heterodimers of Gn andGc, it appeared that with the constructs used, FRET could not be applied for this purpose, as fluorescence from the two fluorophore fusion proteins was never observed in the same cell. This could be due to the fact that interaction between the two glycoproteins interfered with proper folding of (one of) the fluorophores, resulting in greatly reduced and possibly undetectable fluorescence.Another intriguing question-relevant to a broader cell biological field as well-concerns the signal responsible for Golgi localisation of the two glycoproteins during infection. Previous work had shown that Gn carries a Golgi retention signal and is able to rescueGcfrom the ER to the Golgi, suggesting a heterodimerisation of Gn and Gc. For a number of other bunyaviruses, the Golgi retention signal had been mapped to the C-terminal transmembrane domain (TMD) and / or cytoplasmic tail of Gn. Using C-terminal deletion mutants of TSWV Gn and chimeric Gc and vesicular stomatitis virus glycoprotein (VSV-G) constructs (chapter 5), it was shown that both the TMD and the first 30 amino acids of the 60 residues-sized cytoplasmic tail of Gn are necessary for Golgi localisation. The lumenal domain was shown not to be required for Golgi localisation, nor was its presence required for rescuing ofGc. By deletion mapping the 20 most C-terminal residues of the cytoplasmic tail were shown to be crucial for interaction withGc.Large cells containing multiple nuclei were frequently observed whenGcwas expressed. This phenomenon was further investigated in chapter 6, and was shown probably to result from a cell fusion activity of this glycoprotein. Cell fusion is not likely to occur during the plant infection cycle, but may play a role in the infection cycle or the process of virus entry within the thrips vector. The fusion was not pH-dependent and not observed with Gn.Chapter 7 discusses the major findings of this Ph. D. research in a broader perspective, and presents a model for TSWV particle assembly in which all observations have been accomodated.
Tomato spotted wilt virus particle assembly and the prospects of fluorescence microscopy to study protein-protein interactions involved
Snippe, M. ; Goldbach, R.W. ; Kormelink, R.J.M. - \ 2005
Advances in Virus Research 65 (2005). - ISSN 0065-3527 - p. 63 - 122.
resonance energy-transfer - hemorrhagic-fever virus - hantavirus nucleocapsid protein - impatiens necrotic spot - complete nucleotide-sequence - bud necrosis tospovirus - human mxa protein - s-messenger-rna - california encephalitis-virus - double-stranded-rna
This chapter describes the current status of tomato spotted wilt virus (TSWV) particle assembly and the involvement of structural proteins in this process and compares to what is known of the animal-infecting counterparts. It also describes the recently developed fluorescence microscopy techniques that enable the analysis of in vivo protein–protein interactions and how some of these techniques have been employed, as exemplified by recently obtained results, to unravel protein-protein interactions during TSWV particle assembly. Based on the first results on in vivo protein–protein interactions between TSWV structural proteins using fluorescence resonance energy transfer microscopy, it is clear that this and newly developed fluorescence microscopy techniques may become valuable tools not only to unravel the maturation of TSWV and other bunyavirus particles, but also for virology in general to identify and characterize interactions between viral proteins and/or host factors involved in many different processes like replication, transcription, translation, and viral spread.
The use of fluorescence microscopy to visualise homotypic interactions of tomato spotted wilt virus nucleocapsid protein in living cells
Snippe, M. ; Borst, J.W. ; Goldbach, R.W. ; Kormelink, R.J.M. - \ 2005
Journal of Virological Methods 125 (2005)1. - ISSN 0166-0934 - p. 15 - 22.
resonance energy-transfer - plant-cells - fret microscopy - rna segment - n protein - kinase-c - in-situ - identification - phosphorylation - multimerization
Fluorescence resonance energy transfer (FRET) and fluorescence lifetime imaging microscopy (FLIM) were employed to study homotypic protein¿protein interactions in living cells. To this end, the nucleocapsid (N) protein of tomato spotted wilt virus (TSWV) was expressed as a fusion protein with either cyan fluorescent protein (CFP) or yellow fluorescent protein (YFP). Co-expression experiments of the two fusion proteins were carried out in baby hamster kidney (BHK21) cells. Both the wild type and the fusion proteins showed a peri-nuclear localisation pattern and were observed to form aggregates. In sensitised emission experiments, energy transfer was observed to take place from CFP to YFP when the two fluorophores were fused to TSWV N protein, indicating strongly homotypic interaction of the N proteins. This was confirmed by acceptor photobleaching studies as well as by FLIM experiments. All three methods showed interactions taking place, not only in the aggregates in the peri-nuclear region, but also throughout the cytoplasm. These experiments clearly demonstrated the potential of these fluorescence methods for studying the interactions of viral proteins in living cells
|Bewaar TBM-pootgoed bij 3-5 graden
Bus, C.B. ; Snippe, G. - \ 2004
Kennisakker.nl 2004 (2004)15 sep.
pootaardappelen - aardappelen - kiemremmers - kieming - plantengroeiregulatoren - pootknollen - kwaliteit - koudeopslag - koeling - koudebehoefte - akkerbouw - seed potatoes - potatoes - germination inhibitors - germination - plant growth regulators - seed tubers - quality - cold storage - chilling - chilling requirement - arable farming
Op 24 en 25 juni 2004 was er in het kader van Agrobiokon een demonstratie pootgoedkwaliteit op de proefboerderij ’t Kompas. Daar kwamen de bewaaromstandigheden tijdens de opslagperiode van het pootgoed als één van de thema’s aan de orde. De belangrijkste conclusie was dat voor een regelmatig gewas een koele bewaring bij 3 tot 5 graden een belangrijke voorwaarde is. Het maakt hierbij niet uit hoe dit bereikt wordt, als het maar bereikt wordt. Het kan zowel met geforceerde buitenluchtkoeling als met mechanische koeling worden bereikt. Een iets warmere bewaring hoeft geen probleem te zijn, mits de kieming onderdrukt kan worden met een tijdelijke kiemremmer. Er werd getoond: het tijdelijke kiemremmingsmiddel Luxan 4093, mechanische koeling, buitenluchtkoeling, vroeg of laat uit de koeling, contstante hoge temperatuur en vroeg of laat een hoge temperatuur
|In vivo interactions of TSWV structural proteins using fluorescence resonance energy transfer microscopy
Snippe, M. ; Lent, J.W.M. van; Goldbach, R.W. ; Kormelink, R.J.M. - \ 2003
In: XII International Conference on Negative Strand Viruses Pisa : - p. 76 - 76.
|Tomato spotted wilt virus particle assembly in plant and (in) vertebrate cells
Snippe, M. ; Kormelink, R. ; Goldbach, R. - \ 2002
In: The World of Microbes : XIIth International Congress of Virology, Paris - 2002 Paris : EDK Medical and Scientific Int. Publisher - p. 251 - 251.
White spot syndrome virus envelope protein VP28 is involved in the systemic infection of shrimp
Hulten, M.C.W. van; Witteveldt, J. ; Snippe, M. ; Vlak, J.M. - \ 2001
Virology 285 (2001). - ISSN 0042-6822 - p. 228 - 233.
White spot syndrome virus (WSSV) is a large DNA virus infecting shrimp and other crustaceans. The virus particles contain at least five major virion proteins, of which three (VP26, VP24, and VP15) are present in the rod-shaped nucleocapsid and two (VP28 and VP19) reside in the envelope. The mode of entry and systemic infection of WSSV in the black tiger shrimp, Penaeus monodon, and the role of these proteins in these processes are not known. A specific polyclonal antibody was generated against the major envelope protein VP28 using a baculovirus expression vector system. The VP28 antiserum was able to neutralize WSSV infection of P. monodon in a concentration-dependent manner upon intramuscular injection. This result suggests that VP28 is located on the surface of the virus particle and is likely to play a key role in the initial steps of the systemic WSSV infection in shrimp
Epitope polarity and adjuvants influence the fine specificity of the humoral response against Semliki Forest virus specific peptide vaccines
Fernández, I.M. ; Harmsen, M. ; Benaissa-Trouw, B.J. ; Stuij, I. ; Puijk, W. ; Meloen, R.H. ; Snippe, H. ; Kraaijeveld, C.A. - \ 1998
Vaccine 16 (1998). - ISSN 0264-410X - p. 1531 - 1536.
|IgG4 antibodies to pig and cow urinary proteins and respiratory health in Danish swine and dairy farmers.
Doekes, G. ; Snippe, R. ; Iversen, M. ; Heederik, D. - \ 1998
In: 4th International Symposium: Rural Health and Safety in a Changing World, Saskatoon, Canada - p. O78 - O78.
|Werken aan Hoger Onderwijs.
Beijaard, D. ; Snippe, J. ; Bor, W. van den - \ 1996
De Lier : Academisch Boeken Centrum - 153 p.
|Onderzoek inzake buitenlanders in het Nederlandse Hoger Onderwijs; reflectie en vooruitblik.
Bor, W. van den - \ 1994
In: Buitenlandse studenten in het Nederlandse Hoger Onderwijs / Snippe, J., - p. 93 - 104.
|Buitenlandse studenten in het Nederlandse Hoger Onderwijs.
Snippe, J. ; Jochems, W.M.G. ; Bor, W. van den - \ 1994
Delft : Delftse Universitaire Pers - 108
hoger onderwijs - nederland - schoolkinderen - studenten - wereld - buitenlanders - higher education - netherlands - school children - students - world - foreigners