AmpliTaq and AmpliTaq Gold DNA Polymerase - Applied Biosystems

succinyltransferase. Antiserum from a mouse experimentally infected with live Bartonella wasreactive against recombinant SucB, indicating the mounting of an anti-SucB response followinginfection. Antigenic cross-reactivity was observed with antiserum against other Bartonella spp.Antibodies against Coxiella burnetti, Francisella tularensis, and Rickettsia typhi also reacted withour recombinant Bartonella SucB. Potential SucB antigenic cross-reactivity presents a challengeto the development of serodiagnostic tests for other intracellular pathogens that cause diseasessuch as Q fever, rickettsioses, brucelloses, tularemia, and other bartonelloses.Deng, M., T. J. Templeton, et al. (2002). "Cryptosporidium parvum Genes Containing ThrombospondinType 1 Domains." Infect. Immun. 70(12): 6987-6995.http://iai.asm.org/cgi/content/abstract/70/12/6987Cryptosporidium parvum is recognized as an enteropathogen of great worldwide medical andveterinary importance, yet understanding of its pathogenesis has been hampered in part bylimited knowledge of the invasion machinery of this parasite. Recently, genes containingthrombospondin type 1 (TSP1) domains have been identified in several genera of apicomplexans,including thrombospondin-related adhesive proteins (TRAPs) that have been implicated as keymolecules for parasite motility and adhesion onto host cell surfaces. Previously, a large-scalerandom survey of the C. parvum genome conducted in our laboratory revealed the presence ofmultiple genomic DNA sequences with a high degree of similarity to known apicomplexan TRAPgenes. In the present study, TBLASTN screening of available C. parvum genomic sequences byusing TSP1 domains as queries identified a total of 12 genes possessing TSP1-like domains. Allgenes have putative signal peptide sequences, one or more TSP1-like domains, plus additionalextracellular protein modules such as Kringle, epidermal growth factor, and Apple domains. Twogenes, putative paralogs CpTSP8 and CpTSP9, contain predicted introns near their aminotermini, which were verified by comparing PCR products from cDNA versus genomic DNAtemplates. Reverse transcription-PCR analysis of transcript levels reveals that C. parvum TSPgenes were developmentally regulated with distinct patterns of expression during in vitroinfection. TRAPC1, CpTSP3, and CpTSP11 were expressed at high levels during both early andlate stages of infection, whereas CpTSP2, CpTSP5, CpTSP6, CpTSP8, and CpTSP9 weremaximally expressed during the late stages of infection. Only CpTSP4 was highly expressedsolely at an early stage of infection.Papazisi, L., S. Frasca, Jr., et al. (2002). "GapA and CrmA Coexpression Is Essential for Mycoplasmagallisepticum Cytadherence and Virulence." Infect. Immun. 70(12): 6839-6845.http://iai.asm.org/cgi/content/abstract/70/12/6839It was previously demonstrated that avirulent Mycoplasma gallisepticum strain Rhigh (passage164) is lacking three proteins that are expressed in its virulent progenitor, strain Rlow (passage15). These proteins were identified as the cytadhesin molecule GapA, the putative cytadhesinrelatedmolecule CrmA, and a component of a high-affinity transporter system, HatA.Complementation of Rhigh with wild-type gapA restored expression in the transformant (GT5) butdid not restore the cytadherence phenotype and maintained avirulence in chickens. These resultssuggested that CrmA might play an essential role in the M. gallisepticum cytadherence process.CrmA is encoded by the second gene in the gapA operon and shares significant sequencehomology to the ORF6 gene of Mycoplasma pneumoniae, which has been shown to play anaccessory role in the cytadherence process. Complementation of Rhigh with wild-type crmAresulted in the transformant (SDCA) that lacked the cytadherence and virulence phenotypecomparable to that found in Rhigh and GT5. In contrast, complementation of Rhigh with the entirewild-type gapA operon resulted in the transformant (GCA1) that restored cytadherence to the