Synthesis of a Select Group of Proteins by Neisseria Gonorrhoeae in Response to Thermal Stress

Woods, Marion L., Bonfiglioli, Roderick, McGee, Zell A. and Georgopoulos, Costa (1990) Synthesis of a Select Group of Proteins by Neisseria Gonorrhoeae in Response to Thermal Stress. Infection and Immunity, 58 3: 719-725.

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Author Woods, Marion L.
Bonfiglioli, Roderick
McGee, Zell A.
Georgopoulos, Costa
Title Synthesis of a Select Group of Proteins by Neisseria Gonorrhoeae in Response to Thermal Stress
Formatted title
Synthesis of a Select Group of Proteins by Neisseria Gonorrhoeae in Response to Thermal Stress
Journal name Infection and Immunity
ISSN 1098-5522
1070-6313
Publication date 1990-03
Sub-type Article (original research)
Open Access Status File (Publisher version)
Volume 58
Issue 3
Start page 719
End page 725
Total pages 7
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Language eng
Abstract We report the thermal conditions that induce the heat shock response in Neisseria gonorrhoeae. Under conditions of thermal stress, Neisseria gonorrhoeae synthesizes heat shock proteins (hsps), which differ quantitatively from conventionally studied gonococcal proteins. Gonococci accelerate the rate of synthesis of the hsps as early as 5 min after the appropriate stimulus is applied, with synthesis continuing for 30 min, as demonstrated by in vivo labeling experiments with L-[35S]methionine. Two of the gonococcal hsps are immunologically cross-reactive with the hsps of Escherichia coli, DnaK and GroEL, as demonstrated by Western blot (immunoblot) analysis. Ten hsps can be identified on two-dimensional autoradiograms of whole gonococci (total protein). Four hsps can be identified on two-dimensional autoradiograms of 1% N-lauroylsarcosine (sodium salt) (Sarkosyl)-insoluble membrane fractions. Two of the hsps from the 1% Sarkosyl-insoluble fraction are found exclusively in this fraction, suggesting that they are membrane proteins. The identification of this group of proteins will facilitate further study of the function of these proteins and provide insight into the possible role of hsps in disease pathogenesis.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Medicine Publications
 
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