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1.
Food Microbiol ; 28(6): 1111-6, 2011 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-21645808

RESUMEN

Penicillium nordicum is a known contaminant of protein-rich foods and is primarily found on dry-cured meat products. It is an important producer of the mycotoxin ochratoxin A, which has nephrotoxic and cancerogenic activities. Recently a high number of P. nordicum strains was isolated from different dry-cured meat products from one of the Slovenian meat-processing plants. Since we have isolated P. nordicum in high counts also from Artic habitats, such as sea water and sea ice and due to its ability to grow well at low temperatures and at increased salinity, sea salt was suspected as the possible source of P. nordicum. In the present study contamination of meat products, air in the meat-processing plant and sea salt used for salting were analysed. When 50 g of salt sample from a sealed package was dissolved in sterile water and filtered, 12 colonies of P. nordicum were obtained on solid medium incubated at 15 °C, while a salt sample from an open vessel in the meat-processing area developed high, uncountable number of colonies. Amplified fragment length polymorphism analyses of P. nordicum isolates from different sources showed that contamination of meat products via salt was possible. Three selected isolates examined for extrolites all produced ochratoxin A. As contamination of dry-cured meat products with P. nordicum represents a potential health risk for consumers and workers in the meat-processing plants, salt should be taken into account as a potential cause of such contaminations.


Asunto(s)
Contaminación de Alimentos/análisis , Productos de la Carne/microbiología , Micotoxinas/metabolismo , Ocratoxinas/metabolismo , Penicillium/metabolismo , Agua de Mar/microbiología , Animales , Bovinos , Manipulación de Alimentos , Productos de la Carne/análisis , Penicillium/genética , Penicillium/aislamiento & purificación , Cloruro de Sodio/análisis , Cloruro de Sodio/metabolismo , Porcinos
2.
Food Microbiol ; 28(3): 373-6, 2011 May.
Artículo en Inglés | MEDLINE | ID: mdl-21356440

RESUMEN

The surface mycobiota of three types of Slovenian dry-cured meat products were isolated from a total of 75 items of product that were sampled periodically during the drying/ripening stage of processing. The predominant filamentous fungal genus isolated was Penicillium. Eurotium spp., Aspergillus versicolor and Cladosporium spp. were isolated from only two of the products. Eight Penicillium species were identified. Penicillium nordicum was recovered frequently. Penicillium nalgiovense was recovered less frequently, from one product only (a salami), while a yet-to-be described species Penicillium "milanense" was isolated from 21 items. The other penicillia were rarely isolated. Of the isolated and identified species, those that can produce mycotoxins are: A. versicolor, Penicillium brevicompactum, Penicillium chrysogenum, P. nordicum, and Penicillium polonicum. Their growth on dry-cured meat products is undesirable.


Asunto(s)
Seguridad de Productos para el Consumidor , Contaminación de Alimentos/análisis , Manipulación de Alimentos/métodos , Productos de la Carne/microbiología , Penicillium/aislamiento & purificación , Aspergillus/clasificación , Aspergillus/crecimiento & desarrollo , Aspergillus/aislamiento & purificación , Cladosporium/clasificación , Cladosporium/crecimiento & desarrollo , Cladosporium/aislamiento & purificación , Recuento de Colonia Microbiana , Eurotium/clasificación , Eurotium/crecimiento & desarrollo , Eurotium/aislamiento & purificación , Fermentación , Microbiología de Alimentos , Humanos , Penicillium/clasificación , Penicillium/crecimiento & desarrollo , Eslovenia , Especificidad de la Especie
3.
J Virol ; 84(21): 11585-9, 2010 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-20739540

RESUMEN

The human papillomavirus (HPV) minor capsid protein L2 plays important roles in the generation of infectious viral particles and in the initial steps of infection. Here we show that HPV-16 L2 protein is sumoylated at lysine 35 and that sumoylation affects its stability. Interestingly, the sumoylated form of L2 cannot bind to the major capsid protein L1, suggesting a mechanism by which capsid assembly may be modulated in an infected cell. Additionally, L2 appears to modulate the overall sumoylation status of the host cell. These observations indicate a complex interplay between the HPV L2 protein and the host sumoylation machinery.


Asunto(s)
Proteínas de la Cápside/metabolismo , Papillomavirus Humano 16/química , Proteínas Oncogénicas Virales/metabolismo , Proteína SUMO-1/metabolismo , Humanos , Lisina/metabolismo , Unión Proteica , Estabilidad Proteica
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