EspF U nucleic acids and proteins and uses thereof

Details EspF U nucleic acids and proteins and uses thereof EspF U nucleic acids and proteins and uses thereof

2007-07-24

2010-06-08

Monshipouri, Maryam (Department: 1656)

Drug, bio-affecting and body treating compositions

Designated organic active ingredient containing

Peptide containing doai

C530S350000

Reexamination Certificate

active

07732409

ABSTRACT:
Disclosed are EspFU(EspF-like polypeptide encoded by a gene of the cryptic prophage CP-933U of enterohemorrhagicE. coli) polypeptides, fragments thereof, nucleic acids that encode EspFUpolypeptides, or fragments thereof, and cells including the polypeptides, fragments, and/or nucleic acids. Also disclosed are model systems, kits, and methods for screening that use, for example, EspFUpolypeptides and nucleic acids. Also included are pharmaceutical and diagnostic compositions and methods of diagnosis and treatment of EHEC infections.

REFERENCES:
patent: 6365723 (2002-04-01), Blattner et al.
patent: 2003/0023075 (2003-01-01), Blattner et al.
patent: 355074 (2002-12-01), None
Perna et al., UniProt Database, accession No. Q8X482, Mar. 2002.
Bladt et al., “The murine Nck SH2/SH3 adaptors are important for the development of mesoderm-derived embryonic structures and for regulating the cellular actin network,” Mol. Cell Biol. 23:4586-97 (2003).
Campellone and Leong, “Tails of two Tirs: actin pedestal formation by enteropathogenicE. coliand enterohemorrhagicE. coliO157:H7,” Curr. Opin. Microbiol. 6:82-90 (2003).
Campellone et al., “A tyrosine-phosphorylated 12-amino-acid sequence of enteropathogenicEscherichia coliTir binds the host adaptor protein Nck and is required for Nck localization to actin pedestals,” Mol. Microbiol. 43:1227-41 (2002).
Campellone et al., “Clustering of Nck by a 12-residue Tir phosphopeptide is sufficient to trigger localized actin assembly,” J. Cell Biol. 164:407-16 (2004).
Campellone et al., “EspFUis a translocated EHEC effector that interacts with Tir and N-WASP and promotes Nck-independent actin assembly,” Dev. Cell 7:217-28 (2004).
Celli et al., “EnteropathogenicEscherichia coli(EPEC) attachment to epithelial cells: exploiting the host cell cytoskeleton from the outside,” Cell Microbiol. 2:1-9 (2000).
Court et al., “Genetic engineering using homologous recombination,” Annu. Rev. Genet. 36:361-88 (2002).
Crane et al., “Role of EspF in host cell death induced by enteropathogenicEscherichia coli,” Cell. Microbiol. 3:197-211 (2001).
de Grado et al., “Identification of the intimin-binding domain of Tir of enteropathogenicEscherichia coli,” Cell. Microbiol. 1:7-17 (1999).
Deibel et al., “EspE, a novel secreted protein of attaching and effacing bacteria, is directly translocated into infected host cells, where it appears as a tyrosine-phosphorylated 90 kDa protein,” Mol. Microbiol. 28:463-74 (1998).
Desai et al., “The use ofXenopusegg extracts to study mitotic spindle assembly and function in vitro,” Methods Cell. Biol. 61:385-412 (1999).
DeVinney et al., “Enterohaemorrhagic and enteropathogenicEscherichia coliuse a different Tir-based mechanism for pedestal formation,” Mol. Microbiol. 41:1445-58 (2001).
DeVinney et al., “EnterohemorrhagicEscherichia coliO157:H7 produces Tir, which is translocated to the host cell membrane but is not tyrosine phosphorylated,” Infect. Immun. 67:2389-98 (1999).
Donnenberg and Whittam, “Pathogenesis and evolution of virulence in enteropathogenic and enterohemorrhagicEscherichia coli,” J. Clin. Invest. 107:539-48 (2001).
Frankel et al., “Enteropathogenic and enterohaemorrhagicEscherichia coli: more subversive elements,” Mol. Microbiol. 30:911-21(1998).
Goosney et al., “Recruitment of cytoskeletal and signaling proteins to enteropathogenic and enterohemorrhagicEscherichia colipedestals,” Infect. Immun. 69:3315-22 (2001).
Gruenheid et al., “EnteropathogenicE. coliTir binds Nck to initiate actin pedestal formation in host cells,” Nat. Cell. Biol. 3:856-9 (2001).
Hartland et al., “Binding of intimin from enteropathogenicEscherichia colito Tir and to host cells,” Mol. Microbiol. 32:151-8 (1999).
Heng and Cao, “Making cell-permeable antibodies (Transbody) through fusion of protein transduction domains (PTD) with single chain variable fragment (scFv) antibodies: potential advantages over antibodies expressed within the intracellular environment (Intrabody),” Med. Hypotheses 64:1105-8 (2005).
Ho et al., “Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex,” Cell 118:203-16 (2004).
Hudson and Souriau, “Engineered antibodies,” Nat. Med. 9:129-34 (2003).
Kenny et al., “EnteropathogenicE. coli(EPEC) transfers its receptor for intimate adherence into mammalian cells,” Cell 91:511-20 (1997).
Kenny, “Phosphorylation of tyrosine 474 of the enteropathogenicEscherichia coli(EPEC) Tir receptor molecule is essential for actin nucleating activity and is preceded by additional host modifications,” Mol. Microbiol. 31:1229-41 (1999).
Kenny, “The enterohaemorrhagicEscherichia coli(serotype O157:H7) Tir molecule is not functionally interchangeable for its enteropathogenicE. coli(serotype O127:H6) homologue,” Cell. Microbiol. 3:499-510 (2001).
Liu et al., “Point mutants of EHEC intimin that diminish Tir recognition and actin pedestal formation highlight a putative Tir binding pocket,” Mol. Microbiol. 45:1557-73 (2002).
Lommel et al., “Actin pedestal formation by enteropathogenicEscherichia coliand intracellular motility ofShigella flexneriare abolished in N-WASP-defective cells,” EMBO Rep. 2:850-7 (2001).
Lommel et al., “Enterohaemorrhagic and enteropathogenicEscherichia coliuse different mechanisms for actin pedestal formation that converge on N-WASP,” Cell. Microbiol. 6:243-54 (2004).
McNamara et al., “Translocated EspF protein from enteropathogenicEscherichia colidisrupts host intestinal barrier function,” J. Clin. Invest. 107:621-9 (2001).
Mundt et al., “Intrabodies—Valuable tools for target validation,” EBR Winter 2001, ESBA Tech Ed. Jan. 10, 2002.
Murphy and Campellone, “Lambda Red-mediated recombinogenic engineering of enterohemorrhagic and enteropathogenicE. coli,” BMC Mol. Biol. 4:11(2003).
Murphy et al., “PCR-mediated gene replacement inEscherichia coli,” Gene 246:321-30 (2000).
Nataro and Kaper, “DiarrheagenicEscherichia coli,” Clin. Microbiol. Rev. 11:142-201(1998).
Perna et al., “Molecular evolution of a pathogenicity island from enterohemorrhagicEscherichia coliO157:H7,” Infect. Immun. 66:3810-7 (1998).
Peterson et al., “A chemical inhibitor of N-WASP reveals a new mechanism for targeting protein interactions,” Proc. Natl. Acad. Sci. USA 98:10624-9 (2001).
Ritchie et al., “Critical roles forstx2, eae, andtirin enterohemorrhagicEscherichia coli-induced diarrhea and intestinal inflammation in infant rabbits,” Infect. Immun. 71:7129-39 (2003).
Rohatgi et al., “Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway,” J. Biol. Chem. 276:26448-52 (2001).
Tzipori et al., “The role of theeaeAgene in diarrhea and neurological complications in a gnotobiotic piglet model of enterohemorrhagicEscherichia coliinfection,” Infect. Immun. 63:3621-7 (1995).
Viswanathan et al., “Comparative analysis of EspF from enteropathogenic and enterohemorrhagicEscherichia coliin alteration of epithelial barrier function,” Infect. Immun. 72:3218-27 (2004).
Viswanathan et al., “Microbes and their products—physiological effects upon mammalian mucosa,” Adv. Drug Deliv. Rev. 56:727-62 (2004).
Wagner and Waldor, “Bacteriophage control of bacterial virulence,” Infect. Immun. 70:3985-93 (2002).
Restriction Requirement, in U.S. Appl. No. 11/134,563, mailed Nov. 24, 2006 (10 pages).
Fish & Richardson P.C., Response to Restriction Requirement, in U.S. Appl. No. 11/134,563, filed Dec. 22, 2006 (1 page).
Notice of Allowance, in U.S. Appl. No. 11/134,563, mailed Apr. 4, 2007 (14 pages).
Fish & Richardson P.C., Res

Affiliated with

Also associated with

Rating

EspF U nucleic acids and proteins and uses thereof does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with EspF U nucleic acids and proteins and uses thereof, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and EspF U nucleic acids and proteins and uses thereof will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-4198591