Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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    ‘Onze grote droom is een klimaatbestendige boom’
    Copini, P. - \ 2017
    Takkensterfte desastreus voor Nederlandse es
    Copini, P. ; Goudzwaard, L. - \ 2017
    Geen ernstig ongerief
    Niekerk, T.G.C.M. van; Gunnink, H. ; Reuvekamp, B.F.J. - \ 2011
    De Pluimveehouderij 41 (2011)8. - ISSN 0166-8250 - p. 28 - 29.
    pluimveehouderij - dierenwelzijn - kuikens - hanen - dierverzorging - poultry farming - animal welfare - chicks - cocks - care of animals
    In een eerste inventariserende proef heeft Livestock Research gekeken wat de impact van het dubben van kammen is op het kuiken. Het blijkt geen groot probleem voor het dier.
    Climate Change: Global Risks, Challenges and Decisions
    Richardson, K. ; Steffen, W. ; Liverman, D. ; Barker, T. ; Jotzo, F. ; Kammen, D.M. ; Leemans, R. ; Lenton, T.M. ; Munasinghe, M. ; Osman-Elasha, B. ; Schellnhuber, H.J. ; Stern, N. ; Vogel, C. ; Waever, O. - \ 2011
    Cambridge : Cambridge University Press - ISBN 9780521198363 - 524
    klimaatverandering - koolstofcyclus - beleid - mitigatie - risico - klimaat - biofysica - economie - ethiek - climatic change - carbon cycle - policy - mitigation - risk - climate - biophysics - economics - ethics
    Providing an up-to-date synthesis of knowledge relevant to the climate change issue, this book ranges from the basic science documenting the need for policy action to the technologies, economic instruments and political strategies that can be employed in response to climate change. Ethical and cultural issues constraining the societal response to climate change are also discussed. This book covers a very wide range of disciplines – core biophysical sciences involved with climate change (geosciences, atmospheric sciences, ocean sciences, ecology/biology) as well as economics, political science, health sciences, institutions and governance, sociology, ethics and philosophy, and engineering.
    Pilotstudie naar welzijnsaspecten van kammen dubben bij hanen van legrassen = Pilot study welfare implications of dubbing combs of cockerels of Leghorn parent stock
    Niekerk, T.G.C.M. van; Gunnink, H. ; Reuvekamp, B.F.J. - \ 2011
    Lelystad : Wageningen UR Livestock Research (Rapport / Wageningen UR Livestock Research 469)
    pluimveehouderij - kuikens - hanen - chirurgische handelingen - dierenwelzijn - poultry farming - chicks - cocks - surgical operations - animal welfare
    In a small pilot experiment the impact of comb dubbing on male chicks has been investigated. No effect on behaviour, growth and feed intake was recorded, suggesting that dubbing has no major effect on welfare of the chicks.
    Climate Change: global risks challenges and decisions
    Richardson, K. ; Steffen, W. ; Schellnhuber, H.J. ; Alcamo, J. ; Barker, T. ; Kammen, D. ; Leemans, R. ; Liverman, D. ; Monasinghe, M. ; Osman-Elasha, B. ; Stern, N. ; Waever, O. - \ 2009
    Copenhagen, Denmark : University of Copenhagen (Synthesis Report ) - ISBN 9788790655686 - 38
    klimaatverandering - opwarming van de aarde - risicoschatting - milieubeleid - climatic change - global warming - risk assessment - environmental policy
    Intacte sporen hanen nadelig voor welzijn hen : gevolgen toepassen Ingrepenbesluit bij vaccindieren
    Jong, I.C. de; Wolthuis, M. - \ 2006
    De Pluimveehouderij 36 (2006)45. - ISSN 0166-8250 - p. 8 - 9.
    pluimveehouderij - pluimvee - diergedrag - sociale dominantie - hanen - paringsgedrag - dierenwelzijn - voortplanting - bevruchting - beschadigingen - hennen - onderzoeksinstituten - wetenschappelijk onderzoek - poultry farming - poultry - animal behaviour - social dominance - cocks - mating behaviour - animal welfare - reproduction - fertilization - injuries - hens - research institutes - scientific research
    Het toepassen van het Ingrepenbesluit bij hanen (niet kammen dubben, niet tenen knippen en niet sporen branden) heeft nadelig effect op (paar)gedrag en technische resultaten (bevruchting) en zorgt voor beschadiging bij hennen en hanen. Dit blijkt uit onderzoek van ASG bij vaccindieren
    Studies on the C-terminus of the Cowpea mosaic virus movement protein
    Bertens, P. ; Heijne, W. ; Wel, N. van der; Wellink, J.E. ; Kammen, A. van - \ 2003
    Archives of Virology 148 (2003). - ISSN 0304-8608 - p. 265 - 279.
    green fluorescent protein - clover mottle virus - insect cells - tubular structures - subcellular-localization - nsm protein - in-vivo - b-rna - identification - protoplasts
    Cowpea mosaic virus (CPMV) spreads from cell-to-cell as virus particles through tubular structures in modified plasmodesmata which are composed of viral movement protein (MP). Mutational analysis of the MP has revealed that the N-terminal and central regions of the MP are involved in tubule formation and that the C-terminal domain probably has a role in the interactions with virus particles. By constructing C-terminal deletion mutants and comoviral hybrid MPs, it was possible to delineate the C-terminal border of the tubule-forming domain to a small region between amino acids 292 and 298. Experiments with tripartite viruses in protoplasts indicated that the C-terminus of the MP is involved in the incorporation of virus particles in the tubule and that for efficient incorporation of virus particles all MP molecules incorporated in a tubule need to contain a functional C-terminus. A mutant virus coding for a MP in which the last 10 C-terminal amino acids were replaced by the green fluorescent protein (GFP) was able to form tubules in protoplasts. These tubules did not contain virus particles, probably because the GFP interferes with the incorporation of virions into the tubule. These results suggest a model for the structure of the tubule in which the C-terminus of the MP is located inside the tubular structure, where it is able to interact with virus particles.
    Intracellular distribution of cowpea mosaic virus movement protein as visualised by green fluorescent protein fusions
    Gopinath, K. ; Bertens, P. ; Pouwels, J. ; Marks, H. ; Lent, J.W.M. van; Wellink, J.E. ; Kammen, A. van - \ 2003
    Archives of Virology 148 (2003). - ISSN 0304-8608 - p. 2099 - 2144.
    to-cell trafficking - endoplasmic-reticulum - tubular structures - 3a protein - m-rna - protoplasts - plasmodesmata - infection - plants - localization
    Cowpea mosaic virus (CPMV) derivatives expressing movement protein (MP) green fluorescent protein (GFP) fusions (MP:GFP) were used to study the intracellular targeting and localization of the MP in cowpea protoplasts and plants. In protoplasts, a virus coding for a wild type MP:GFP (MPfGFP) induced the formation of fluorescent tubular structures, which shows that subcellular targeting and tubule formation are not affected by fusion of GFP to the C-terminus of the MP. In plants, MPfGFP infections were mostly confined to single epidermal cells and failed to achieve a systemic infection, probably because the fusion of GFP to the MP interfered with MP-virion interaction. MP:GFP mainly accumulated in fluorescent spots in the cell wall of epidermal cells of inoculated leaves, which may represent short tubular structures in modified plasmodesmata. At the cuticle-side of epidermal cells tubular structures were detected indicating that tubule formation in plants, as in protoplasts, does not require the presence of functional plasmodesmata. Furthermore, results were obtained which indicate that CPMV MP:GFP is able to traffic from cell-to-cell by itself. The possible significance of this finding is discussed.
    Transgenic plants expressing HC-Pro show enhanced virus sensitivity while silencing of the transgene results in resistance
    Mlotshwa, S. ; Verver, J. ; Sithole-Niang, I. ; Prins, M. ; Kammen, A. van; Wellink, J. - \ 2002
    Virus Genes 25 (2002)1. - ISSN 0920-8569 - p. 45 - 47.
    Nicotiana benthamiana plants were engineered to express sequences of the helper component-proteinase (HC-Pro) of Cowpea aphid-borne mosaic potyvirus (CABMV). The sensitivity of the transgenic plants to infection with parental and heterologous viruses was studied. The lines expressing HC-Pro showed enhanced symptoms after infection with the parental CABMV isolate and also after infection with a heterologous potyvirus, Potato virus Y (PVY) and a comovirus, Cowpea mosaic virus (CPMV). On the other hand, transgenic lines expressing nontranslatable HC-Pro or translatable HC-Pro with a deletion of the central domain showed wild type symptoms after infection with the parental CABMV isolate and heterologous viruses. These results showed that CABMV HC-Pro is a pathogenicity determinant that conditions enhanced sensitivity to virus infection in plants, and that the central domain of the protein is essential for this. The severe symptoms in CABMV-infected HC-Pro expressing lines were remarkably followed by brief recovery and subsequent re-establishment of infection, possibly indicating counteracting effects of HC-Pro expression and a host defense response. One of the HC-Pro expressing lines (h48) was found to contain low levels of transgenic HC-Pro RNA and to be resistant to CABMV and to recombinant CPMV expressing HC-Pro. This indicated that h48 was (partially) posttranscriptionally silenced for the HC-Pro transgene inspite of the established role of HC-Pro as a suppressor of posttranscriptional gene silencing. Line h48 was not resistant to PVY, but instead showed enhanced symptoms compared to nontransgenic plants. This may be due to relief of silencing of the HC-Pro transgene by HC-Pro expressed by PVY.
    Cowpea mosaic virus 32- and 60-kilodalton replication proteins target and change the morphology of endoplasmic reticulum membranes
    Carette, J.E. ; Lent, J. van; MacFarlance, S.A. ; Wellink, J.E. ; Kammen, A. van - \ 2002
    Journal of Virology 76 (2002). - ISSN 0022-538X - p. 6293 - 6301.
    green fluorescent protein - high-level synthesis - b-rna - poliovirus infection - viral replication - golgi membranes - 2bc - plants - cells - proliferation
    Cowpea mosaic virus (CPMV) replicates in close association with small membranous vesicles that are formed by rearrangements of intracellular membranes. To determine which of the viral proteins are responsible for the rearrangements of membranes and the attachment of the replication complex, we have expressed individual CPMV proteins encoded by RNA1 in cowpea protoplasts by transient expression and in Nicotiana benthamiana plants by using the tobacco rattle virus (TRV) expression vector. The 32-kDa protein (32K) and 60K, when expressed individually, accumulate in only low amounts but are found associated with membranes mainly derived from the endoplasmic reticulum (ER). 24K and 110K are freely soluble and accumulate to high levels. With the TRV vector, expression of 32K and 60K results in rearrangement of ER membranes. Besides, expression of 32K and 60K results in necrosis of the inoculated N. benthamiana leaves, suggesting that 32K and 60K are cytotoxic proteins. On the other hand, during CPMV infection 32K and 60K accumulate to high levels without causing necrosis.
    Subcellular location of the helper component-proteinase of Cowpea Aphid-Borne Mosaic Virus
    Mlotshwa, S. ; Verver, J. ; Sithole-Niang, I. ; Gopinath, K. ; Carette, J. ; Kammen, A. van; Wellink, J. - \ 2002
    Virus Genes 25 (2002)2. - ISSN 0920-8569 - p. 207 - 216.
    The helper component-proteinase (HC-Pro) of Cowpea aphid-borne mosaic virus (CABMV) was expressed in Escherichia coli and used to obtain HC-Pro antiserum that was used as an analytical tool for HC-Pro studies. The antiserum was used in immunofluorescence assays to study the subcellular location of HC-Pro expressed with other viral proteins in cowpea protoplasts in a natural CABMV infection, or in protoplasts transfected with a transient expression construct expressing HC-Pro separately from other viral proteins under the control of the 35S promoter. In both cases the protein showed a diffuse cytoplasmic location. Similar localisation patterns were shown in live protoplasts when the transient expression system was used to express HC-Pro as a fusion with the green fluorescent protein as a reporter. In an alternative expression system, the HC-Pro coding region was subcloned in-frame between the movement protein and large coat protein genes of RNA2 of Cowpea mosaic virus (CPMV). Upon transfection of protoplasts with this construct, HC-Pro was expressed as part of the RNA2 encoded polyprotein from which it was fully processed. In this case, the protein localised in broad cytoplasmic patches reminiscent of the typical CPMV induced cytopathic structures in which CPMV replication occurs, suggesting an interaction of HC-Pro with CPMV proteins or host factors in these structures. Finally, recombinant CPMV expressing HC-Pro showed a strongly enhanced virulence on cowpea and Nicotiana benthamiana consistent with the role of HC-Pro as a pathogenicity determinant, a phenomenon now known to be linked to its role as a suppressor of host defense responses based on post-transcriptional gene silencing.
    The genomic sequence of cowpea aphid-borne mosaic virus and its similarities with other potyviruses
    Mlotshwa, S. ; Verver, J. ; Sithole-Niang, I. ; Kampen, T. van; Kammen, A. van; Wellink, J. - \ 2002
    Archives of Virology 147 (2002). - ISSN 0304-8608 - p. 1043 - 1052.
    The genomic sequence of a Zimbabwe isolate of Cowpea aphid-borne mosaic virus (CABMV-Z) was determined by sequencing overlapping viral cDNA clones generated by RT-PCR using degenerate and/or specific primers. The sequence is 9465 nucleotides in length excluding the 3' terminal poly (A) tail and contains a single open reading frame (ORF) of 9159 nucleotides encoding a large polyprotein of 3 053 amino acids and predicted Mr of 348. The size of the genome and the encoded polyprotein is in agreement with other potyviruses and contains nine putative proteolytic cleavage sites and motifs conserved in homologous proteins of other potyviruses. The P1 and P3 were the most variable proteins while CI, NIb and CP were the most conserved.
    A relationship between seed development, Arabinogalactan-proteins (AGPs) and the AGP mediated promotion of somatic embryogenesis
    Hengel, A.J. van; Kammen, A. van; Vries, S.C. de - \ 2002
    Physiologia Plantarum 114 (2002). - ISSN 0031-9317 - p. 637 - 644.
    Arabinogalactan-protein (AGP) epitopes are known to display developmentally regulated patterns of expression in several plant tissues. Therefore, AGPs have been suggested to play a role in plant development. Somatic embryogenesis is regulated by AGPs as well as by EP3 endochitinases. Using four different methods we have analysed the composition of AGPs in immature carrot seeds. The results obtained show that: (1) the native electrophoretic mobility of such AGPs changes during development; (2) AGP epitopes in immature seeds are developmentally regulated; (3) enzymatically released fragments of AGPs show that the composition of these molecules changes as a function of development; and (4) the biological activity of AGPs on the formation of somatic embryos changes depending on the age of the seeds. Our results suggest that degradation of maternally derived AGPs occurs after fertilization, while cellularization of the endosperm leads to synthesis of a new set of AGPs. The presence of an endochitinase cleavage site as well as the capacity to increase somatic embryogenesis only occurred in AGPs that were isolated from seeds in which the endosperm had been cellularized. Apparently, both EP3 endochitinases and somatic embryogenesis-promoting AGPs are developmentally regulated in immature carrot seeds.
    Coalescence of the sites of cowpea mosaic virus RNA replication into a cytopathic structure
    Carette, J.E. ; Gühl, K. ; Wellink, J. ; Kammen, A. van - \ 2002
    Journal of Virology 76 (2002)12. - ISSN 0022-538X - p. 6235 - 6243.
    Cowpea mosaic virus (CPMV) replication induces an extensive proliferation of endoplasmic reticulum (ER) membranes, leading to the formation of small membranous vesicles where viral RNA replication takes place. Using fluorescent in situ hybridization, we found that early in the infection of cowpea protoplasts, CPMV plus-strand RNA accumulates at numerous distinct subcellular sites distributed randomly throughout the cytoplasm which rapidly coalesce into a large body located in the center of the cell, often near the nucleus. The combined use of immunostaining and a green fluorescent protein ER marker revealed that during the course of an infection, CPMV RNA colocalizes with the 110-kDa viral polymerase and other replication proteins and is always found in close association with proliferated ER membranes, indicating that these sites correspond to the membranous site of viral replication. Experiments with the cytoskeleton inhibitors oryzalin and latrunculin B point to a role of actin and not tubulin in establishing the large central structure. The induction of ER membrane proliferations in CPMV-infected protoplasts did not coincide with increased levels of BiP mRNA, indicating that the unfolded-protein response is not involved in this process
    Characterization of plant proteins that interact with cowpea mosaic virus ‘60K’ protein in the yeast two-hybrid system
    Carette, J.E. ; Verver, J. ; Martens, J. ; Kampen, T. van; Wellink, J. ; Kammen, A. van - \ 2002
    Journal of General Virology 83 (2002). - ISSN 0022-1317 - p. 885 - 893.
    Origin of the membrane compartment for cowpea mosaic virus RNA replication
    Carette, J.E. - \ 2002
    Wageningen University. Promotor(en): A. van Kammen; J. Wellink. - S.l. : S.n. - ISBN 9789058085573 - 120
    koebonenmozaïekvirus - dna-replicatie - membranen - vigna unguiculata - vignabonen - blaasjes - virusreplicatie - plantenziekten - cowpea mosaic virus - dna replication - membranes - vigna unguiculata - cowpeas - vesicles - viral replication - plant diseases

    Replication of many positive-stranded RNA viruses takes place in association with intracellular membranes. Often these membranes are induced upon infection by vesiculation or rearrangement of membranes from different organelles including the early and late endomembrane system. Upon infection of cowpea cells with cowpea mosaic virus (CPMV) typical cytopathological structures are formed, which consist of an amorphous matrix of electron-dense material traversed by rays of small membranous vesicles. This thesis describes the studies that were undertaken to define the cellular components involved in the establishment of the site of viral RNA replication consisting of vesiculated membranes and electron-dense material. Furthermore, the role of individual viral proteins as well as host proteins in this process was investigated.

    Mutational analysis of the genome-linked protein of cowpea mosaic virus
    Carette, J.E. ; Kujawa, A. ; Gühl, K. ; Verver, J. ; Wellink, J. ; Kammen, A. van - \ 2001
    Virology 290 (2001). - ISSN 0042-6822 - p. 21 - 29.
    In this study we have performed a mutational analysis of the cowpea mosaic comovirus (CPMV) genome-linked protein VPg to discern the structural requirements necessary for proper functioning of VPg. Either changing the serine residue linking VPg to RNA at a tyrosine or a threonine or changing the position of the serine from the N-terminal end to position 2 or 3 abolished virus infectivity. Some of the mutations affected the cleavage between the VPg and the 58K ATP-binding protein in vitro, which might have contributed to the lethal phenotype. RNA replication of some of the mutants designed to replace VPg with the related cowpea severe mosaic comovirus was completely abolished, whereas replication of others was not affected or only mildly affected, showing that amino acids that are not conserved between the comoviruses can be critical for the function of VPg. The replicative proteins of one of the mutants failed to accumulate in typical cytopathic structures and this might reflect the involvement of VPg in protein–protein interactions with the other replicative proteins.
    N-acetylglucosamine and glucosamine-containing arabinogalactan proteins control somatic embryogenesis
    Hengel, A.J. van; Tadesse, Z. ; Immerzeel, P. ; Schols, H. ; Kammen, A. van; Vries, S.C. de - \ 2001
    Plant Physiology 125 (2001). - ISSN 0032-0889 - p. 1880 - 1890.
    In plants, complete embryos can develop not only from the zygote, but also from somatic cells in tissue culture. How somatic cells undergo the change in fate to become embryogenic is largely unknown. Proteins, secreted into the culture medium such as endochitinases and arabinogalactan proteins (AGPs) are required for somatic embryogenesis. Here we show that carrot (Daucus carota) AGPs can contain glucosamine and N-acetyl-D-glucosaminyl and are sensitive to endochitinase cleavage. To determine the relevance of this observation for embryogenesis, an assay was developed based on the enzymatic removal of the cell wall from cultured cells. The resulting protoplasts had a reduced capacity for somatic embryogenesis, which could be partially restored by adding endochitinases to the protoplasts. AGPs from culture medium or from immature seeds could fully restore or even increase embryogenesis. AGPs pretreated with chitinases were more active than untreated molecules and required an intact carbohydrate constituent for activity. AGPs were only capable of promoting embryogenesis from protoplasts in a short period preceding cell wall reformation. Apart from the increase in embryogenesis, AGPs can reinitiate cell division in a subpopulation of otherwise non-dividing protoplasts. These results show that chitinase-modified AGPs are extracellular matrix molecules able to control or maintain plant cell fate.
    Cowpea aphid-borne mosaic potyvirus (CABMV)
    Mlotshwa, S. ; Sithole-Niang, I. ; Kammen, A. van; Wellink, J. - \ 2000
    In: Research advances in virology / Mohan, R.M., Kerala : Global Research Network - ISBN 9788187736110 - p. 127 - 136.
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