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  • American Society for Microbiology  (2)
  • 2005-2009  (2)
  • 1
    In: Journal of Virology, American Society for Microbiology, Vol. 83, No. 7 ( 2009-04), p. 2883-2891
    Abstract: Entry of ebolavirus (EBOV) into cells is mediated by its glycoprotein (GP 1,2 ), a class I fusion protein whose structure was recently determined (J. E. Lee et al., Nature 454: 177-182, 2008). Here we confirmed two major predictions of the structural analysis, namely, the residues in GP 1 and GP 2 that remain after GP 1,2 is proteolytically primed by endosomal cathepsins for fusion and residues in GP 1 that are critical for binding to host cells. Mass spectroscopic analysis indicated that primed GP 1,2 contains residues 33 to 190 of GP 1 and all residues of GP 2 . The location of the receptor binding site was determined by a two-pronged approach. We identified a small receptor binding region (RBR), residues 90 to 149 of GP 1 , by comparing the cell binding abilities of four RBR proteins produced in high yield. We characterized the binding properties of the optimal RBR (containing GP 1 residues 57 to 149) and then conducted a mutational analysis to identify critical binding residues. Substitutions at four lysines (K95, K114, K115, and K140) decreased binding and the ability of RBR proteins to inhibit GP 1,2 -mediated infection. K114, K115, and K140 lie in a small region modeled to be located on the top surface of the chalice following proteolytic priming; K95 lies deeper in the chalice bowl. Combined with those of Lee et al., our findings provide structural insight into how GP 1,2 is primed for fusion and define the core of the EBOV RBR (residues 90 to 149 of GP 1 ) as a highly conserved region containing a two-stranded β-sheet, the two intra-GP 1 disulfide bonds, and four critical Lys residues.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2009
    detail.hit.zdb_id: 1495529-5
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  • 2
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 187, No. 18 ( 2005-09-15), p. 6488-6498
    Abstract: Pseudomonas syringae pv. phaseolicola, a gram-negative bacterial plant pathogen, is the causal agent of halo blight of bean. In this study, we report on the genome sequence of P. syringae pv. phaseolicola isolate 1448A, which encodes 5,353 open reading frames (ORFs) on one circular chromosome (5,928,787 bp) and two plasmids (131,950 bp and 51,711 bp). Comparative analyses with a phylogenetically divergent pathovar, P. syringae pv. tomato DC3000, revealed a strong degree of conservation at the gene and genome levels. In total, 4,133 ORFs were identified as putative orthologs in these two pathovars using a reciprocal best-hit method, with 3,941 ORFs present in conserved, syntenic blocks. Although these two pathovars are highly similar at the physiological level, they have distinct host ranges; 1448A causes disease in beans, and DC3000 is pathogenic on tomato and Arabidopsis . Examination of the complement of ORFs encoding virulence, fitness, and survival factors revealed a substantial, but not complete, overlap between these two pathovars. Another distinguishing feature between the two pathovars is their distinctive sets of transposable elements. With access to a fifth complete pseudomonad genome sequence, we were able to identify 3,567 ORFs that likely comprise the core Pseudomonas genome and 365 ORFs that are P. syringae specific.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2005
    detail.hit.zdb_id: 1481988-0
    SSG: 12
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