Survival of Salmonella on Tomatoes Stored at High Relative Humidity, in Soil, and on Tomatoes in Contact with Soil

2002 ◽  
Vol 65 (2) ◽  
pp. 274-279 ◽  
Author(s):  
XUAN GUO ◽  
JINRU CHEN ◽  
ROBERT E. BRACKETT ◽  
LARRY R. BEUCHAT

Salmonellosis has been linked to the consumption of several types of raw fruits and vegetables, some of which may have been contaminated with Salmonella before harvesting. The objectives of this study were to investigate water and soil as reservoirs of Salmonella for the contamination of mature green tomato fruits. Salmonella survived for at least 45 days in inoculated moist soil. The population of Salmonella on tomatoes in contact with soil increased by 2.5 log10 CFU per tomato during storage for 4 days at 20°C and remained constant for an additional 10 days. The number of cells inoculated on tomatoes decreased by approximately 4 log10 CFU per tomato during storage for 14 days at 20°C and 70% relative humidity. Fruits in contact with inoculated soil for 1 day at 20°C harbored Salmonella only near or on the skin surface. More Salmonella cells were observed in stem scar and subsurface areas of tomatoes as the time of storage increased. PCR fingerprinting revealed that among five Salmonella serotypes in the inoculum, Salmonella Montevideo was the most persistent on tomatoes in contact with inoculated soil and on spot-inoculated tomatoes, followed by Salmonella Poona and Salmonella Michigan. The results of this study demonstrate that an enhanced green fluorescent protein marker can be used to detect cells and monitor the growth of Salmonella in the presence of other microorganisms. Observations on the infiltration of Salmonella into tomato tissues support the contention that preharvest contact of produce with contaminated water or soil exacerbates problems associated with the postharvest removal of pathogens or their accessibility to treatment with sanitizers.

2006 ◽  
Vol 14 (21) ◽  
pp. 9815 ◽  
Author(s):  
Alberto Diaspro ◽  
Silke Krol ◽  
Barbara Campanini ◽  
Fabio Cannone ◽  
Giuseppe Chirico

Viruses ◽  
2021 ◽  
Vol 13 (4) ◽  
pp. 632
Author(s):  
Yingyun Cai ◽  
Shuiqing Yu ◽  
Ying Fang ◽  
Laura Bollinger ◽  
Yanhua Li ◽  
...  

Simian hemorrhagic fever virus (SHFV) causes acute, lethal disease in macaques. We developed a single-plasmid cDNA-launch infectious clone of SHFV (rSHFV) and modified the clone to rescue an enhanced green fluorescent protein-expressing rSHFV-eGFP that can be used for rapid and quantitative detection of infection. SHFV has a narrow cell tropism in vitro, with only the grivet MA-104 cell line and a few other grivet cell lines being susceptible to virion entry and permissive to infection. Using rSHFV-eGFP, we demonstrate that one cricetid rodent cell line and three ape cell lines also fully support SHFV replication, whereas 55 human cell lines, 11 bat cell lines, and three rodent cells do not. Interestingly, some human and other mammalian cell lines apparently resistant to SHFV infection are permissive after transfection with the rSHFV-eGFP cDNA-launch plasmid. To further demonstrate the investigative potential of the infectious clone system, we introduced stop codons into eight viral open reading frames (ORFs). This approach suggested that at least one ORF, ORF 2b’, is dispensable for SHFV in vitro replication. Our proof-of-principle experiments indicated that rSHFV-eGFP is a useful tool for illuminating the understudied molecular biology of SHFV.


2000 ◽  
Vol 113 (21) ◽  
pp. 3761-3768 ◽  
Author(s):  
I. Jagiello ◽  
A. Van Eynde ◽  
V. Vulsteke ◽  
M. Beullens ◽  
A. Boudrez ◽  
...  

NIPP1 is a nuclear subunit of protein phosphatase-1 (PP1) that colocalizes with pre-mRNA splicing factors in speckles. We report here that the nuclear and subnuclear targeting of NIPP1, when expressed in HeLa cells or COS-1 cells as a fusion protein with the enhanced-green-fluorescent protein (EGFP), are mediated by distinct sequences. While NIPP1-EGFP can cross the nuclear membrane passively, the active transport to the nucleus is mediated by two independent nuclear localization signals in the central domain of NIPP1, which partially overlap with binding site(s) for PP1. Furthermore, the concentration of NIPP1-EGFP in the nuclear speckles requires the ‘ForkHead-Associated’ domain in the N terminus. This domain is also required for the nuclear retention of NIPP1 when active transport is blocked. Our data imply that the nuclear and subnuclear targeting of NIPP1 are controlled independently.


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