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1
Gaywee J, Xu W-L, Radulovic S, Bessman MJ, Azad AF, 2002. The Rickettsia prowazekii invasion gene homolog (invA) encodes a nudix hydrolase active on adenosine (5′)-pentaphospho-(5′)-adenosine. Mol Cell Proteomics 1 :179–185.
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2
Lee PC, Bochner BR, Ames BN, 1983. AppppA, heat shock stress, and cell oxidation. Proc Natl Acad Sci U S A 80 :7496–7500.
-
3
Bochner BR, Lee PC, Wilson SW, Cutler CW, Ames BN, 1984. AppppA and related adenylated nucleotides are synthesized as a consequence of oxidative stress. Cell. 37 :225–232.
-
4
McLennan AG, 2000. Dinucleoside polyphosphates-friend or foe? Pharmacol Ther 87 :73–89.
-
5
Guranowski A, 2000. Specific and nonspecific enzymes involved in the catabolism of mono- and dinucleoside polyphosphates. Pharmacol Ther 87 :117–139.
-
6
Mateo J, Miras-Portugal MT, Rotllan P, 1997. Ecto-enzymatic hydrolysis of diadenosine polyphosphates by cultured adrenomedullary vascular endothelial cells. Am J Physiol 273 :C918–C927.
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7
Von Drygalski A, Ogilvie A, 2000. Ecto-diadenosine 5′,5′′′- P1,P4-tetraphosphate (Ap4A)-hydrolase is expressed as an ectoenzyme in a variety of mammalian cells and adds new aspects to the turnover of Ap4A. Biofactors 11 :179–187.
-
8
Aguilar JS, Reyes R, Asensio AC, Oakin S, Rotllan P, Miledi R, 2001. Ectoenzymatic breakdown of diadenosine polyphosphates by Xenopus laevis oocytes. Eur J Biochem 268 :1289–1297.
-
9
Feussner K, Guranowski A, Kostka S, Wasternack C, 1996. Diadenosine 5′,5′′′-P1,P4-tetraphosphate (Ap4A) hydrolase from tomato (Lycopersicon esculentum cv. Lukullus)—purification, biochemical properties and behaviour during stress. Zeitschr Naturforsch Section C J Biosci 51 :477–486.
-
10
Nielsen H, Engelbrecht J, Brunak S, Von Heijne G, 1997. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 10 :1–6.
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11
Radulovic S, Feng HM, Morovic M, Djelalija B, Popov V, Crocquet-Valdes P, Walker DH, 1996. Isolation of Rickettsia akari from the patient in a region where Mediterranean spotted fever is endemic. Clin Infect Dis 22 :216–220.
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12
Manor E, Carbonetti NH, Silverman DJ, 1994. Rickettsia rickettsii has proteins with cross-reacting epitopes to eukaryotic phospholipase A2 and phospholipase C. Microb Pathog 17 :99–109.
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SUBCELLULAR LOCALIZATION OF RICKETTSIAL INVASION PROTEIN, INVA
JARIYANART GAYWEE
JARIYANART GAYWEE
Department of Microbiology and Immunology, School of Medicine, University of Maryland, Baltimore, Maryland
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JOHN B. SACCI JR
JOHN B. SACCI JR
Department of Microbiology and Immunology, School of Medicine, University of Maryland, Baltimore, Maryland
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SUZANA RADULOVIC
SUZANA RADULOVIC
Department of Microbiology and Immunology, School of Medicine, University of Maryland, Baltimore, Maryland
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MAGDA S. BEIER
MAGDA S. BEIER
Department of Microbiology and Immunology, School of Medicine, University of Maryland, Baltimore, Maryland
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ABDU F. AZAD
ABDU F. AZAD
Department of Microbiology and Immunology, School of Medicine, University of Maryland, Baltimore, Maryland
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To understand further the molecular basis of rickettsial host cell invasion, Rickettsia prowazekii invasion gene homolog (invA) has been characterized. Our previous experiments have shown that InvA is an Ap5A pyrophosphatase, a member of the Nudix hydrolase family, which is up-regulated during the internalization, early growth phase, and exit steps during rickettsial mammalian cell infection. In addition to the molecular characterization, subcellular localization of InvA was investigated. InvA-specific antibodies were raised in mice and used for immunoelectron microscopy. The generated antibodies were shown to recognize InvA and by immunogold labeling showed InvA in the cytoplasm of rickettsiae. A cytoplasmic location for InvA would allow for a rapid response to any internal substance and efficient functioning in hydrolysis of toxic metabolic by-products that are accumulated in the rickettsial cytoplasm during host cell invasion. Protecting bacteria from a hazardous environment could enhance their viability and allow them to remain metabolically active, which is a necessary step for the rickettsial obligate intracellular lifestyle.
Author Notes
ProCite
RefWorks
Reference Manager
BibTeX
Zotero
EndNote
-
1
Gaywee J, Xu W-L, Radulovic S, Bessman MJ, Azad AF, 2002. The Rickettsia prowazekii invasion gene homolog (invA) encodes a nudix hydrolase active on adenosine (5′)-pentaphospho-(5′)-adenosine. Mol Cell Proteomics 1 :179–185.
-
2
Lee PC, Bochner BR, Ames BN, 1983. AppppA, heat shock stress, and cell oxidation. Proc Natl Acad Sci U S A 80 :7496–7500.
-
3
Bochner BR, Lee PC, Wilson SW, Cutler CW, Ames BN, 1984. AppppA and related adenylated nucleotides are synthesized as a consequence of oxidative stress. Cell. 37 :225–232.
-
4
McLennan AG, 2000. Dinucleoside polyphosphates-friend or foe? Pharmacol Ther 87 :73–89.
-
5
Guranowski A, 2000. Specific and nonspecific enzymes involved in the catabolism of mono- and dinucleoside polyphosphates. Pharmacol Ther 87 :117–139.
-
6
Mateo J, Miras-Portugal MT, Rotllan P, 1997. Ecto-enzymatic hydrolysis of diadenosine polyphosphates by cultured adrenomedullary vascular endothelial cells. Am J Physiol 273 :C918–C927.
-
7
Von Drygalski A, Ogilvie A, 2000. Ecto-diadenosine 5′,5′′′- P1,P4-tetraphosphate (Ap4A)-hydrolase is expressed as an ectoenzyme in a variety of mammalian cells and adds new aspects to the turnover of Ap4A. Biofactors 11 :179–187.
-
8
Aguilar JS, Reyes R, Asensio AC, Oakin S, Rotllan P, Miledi R, 2001. Ectoenzymatic breakdown of diadenosine polyphosphates by Xenopus laevis oocytes. Eur J Biochem 268 :1289–1297.
-
9
Feussner K, Guranowski A, Kostka S, Wasternack C, 1996. Diadenosine 5′,5′′′-P1,P4-tetraphosphate (Ap4A) hydrolase from tomato (Lycopersicon esculentum cv. Lukullus)—purification, biochemical properties and behaviour during stress. Zeitschr Naturforsch Section C J Biosci 51 :477–486.
-
10
Nielsen H, Engelbrecht J, Brunak S, Von Heijne G, 1997. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 10 :1–6.
-
11
Radulovic S, Feng HM, Morovic M, Djelalija B, Popov V, Crocquet-Valdes P, Walker DH, 1996. Isolation of Rickettsia akari from the patient in a region where Mediterranean spotted fever is endemic. Clin Infect Dis 22 :216–220.
-
12
Manor E, Carbonetti NH, Silverman DJ, 1994. Rickettsia rickettsii has proteins with cross-reacting epitopes to eukaryotic phospholipase A2 and phospholipase C. Microb Pathog 17 :99–109.
| Past two years | Past Year | Past 30 Days | |
|---|---|---|---|
| Abstract Views | 262 | 239 | 20 |
| Full Text Views | 319 | 2 | 0 |
| PDF Downloads | 32 | 2 | 0 |