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Proteomic analysis of Listeria monoc...

Mujahid, Sana.

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Proteomic analysis of Listeria monocytogenes.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Proteomic analysis of Listeria monocytogenes./
作者:	Mujahid, Sana.
面頁冊數:	117 p.
附註:	Adviser: Chinling Wang.
Contained By:	Masters Abstracts International46-04.
標題:	Biology, Microbiology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1451423
ISBN:	9780549411871

Proteomic analysis of Listeria monocytogenes.
Mujahid, Sana.

Proteomic analysis of Listeria monocytogenes. - 117 p.

Adviser: Chinling Wang.

Thesis (M.S.)--Mississippi State University, 2008.

Listeria monocytogenes is a deadly, Gram-positive foodborne pathogen that is ubiquitous in the environment. The bacterium expresses a number of virulence and stress adaptation proteins that support its pathogenic capabilities. Two-dimensional gel electrophoresis (2-DE) was used to map L. monocytogenes surface proteins, which play a central role in virulence, and to examine protein expression by L. monocytogenes grown on ready-to-eat meat, an important source of Listeria infections. A novel method for solubilization of surface proteins from L. monocytogenes for 2-DE was developed. Additionally, the unique proteome expressed by L. monocytogenes grown on a meat matrix was uncovered. The developed solubilization method will facilitate efforts to identify and routinely compare surface proteins of Listeria by 2-DE. Furthermore, the 2-DE database of proteins expressed by L. monocytogenes grown on a meat matrix will allow further understanding of the interactions of Listeria with its food environment that influence its ability to cause disease.

ISBN: 9780549411871Subjects--Topical Terms:

1017734
Biology, Microbiology.

Proteomic analysis of Listeria monocytogenes.
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520 $a Listeria monocytogenes is a deadly, Gram-positive foodborne pathogen that is ubiquitous in the environment. The bacterium expresses a number of virulence and stress adaptation proteins that support its pathogenic capabilities. Two-dimensional gel electrophoresis (2-DE) was used to map L. monocytogenes surface proteins, which play a central role in virulence, and to examine protein expression by L. monocytogenes grown on ready-to-eat meat, an important source of Listeria infections. A novel method for solubilization of surface proteins from L. monocytogenes for 2-DE was developed. Additionally, the unique proteome expressed by L. monocytogenes grown on a meat matrix was uncovered. The developed solubilization method will facilitate efforts to identify and routinely compare surface proteins of Listeria by 2-DE. Furthermore, the 2-DE database of proteins expressed by L. monocytogenes grown on a meat matrix will allow further understanding of the interactions of Listeria with its food environment that influence its ability to cause disease.
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