Identification and molecular characterisation of a fibrinogen binding protein from .-1

Ransferred to PVDF, then membranes were probed with streptavidin-alkaline phosphatase conjugate and developed with NBT/BCIP. Panel A) Lanes 1 and 2 comprised 5 μl cells grown in vegetable peptone, whilst lanes 2 and 3 contained 5 μl cells grown in barramundi serum. Cells were harvested and washed in TBS before being incubated with biotinylated human fibrinogen (Lanes 1 and 3) or TBS (lanes 2 and 4) for 20 min, prior to extensive washing and transfer onto PVDF membrane for subsequent detection. Fb indicates serial two-fold dilutions of biotinylated fibrinogen commencing at 2.5 μg/mL. Panel B) shows serial 2 × dilutions of 5 μl cells diluted in TBS. Lane F, cells incubated first with TBS then with biotinylated fibrinogen before transfer to the membrane. Lane P+F, cells incubated with barramundi plasma followed by biotinylated fibrinogen, Lane TBS, cells incubated twice in TBS.<p><b>Copyright information:</b></p><p>Taken from "Identification and molecular characterisation of a fibrinogen binding protein from ."</p><p>http://www.biomedcentral.com/1471-2180/8/67</p><p>BMC Microbiology 2008;8():67-67.</p><p>Published online 23 Apr 2008</p><p>PMCID:PMC2387161.</p><p></p

Identification and molecular characterisation of a fibrinogen binding protein from .-2

And the respiratory burst was measured by luminol-enhanced chemiluminescence.<p><b>Copyright information:</b></p><p>Taken from "Identification and molecular characterisation of a fibrinogen binding protein from ."</p><p>http://www.biomedcentral.com/1471-2180/8/67</p><p>BMC Microbiology 2008;8():67-67.</p><p>Published online 23 Apr 2008</p><p>PMCID:PMC2387161.</p><p></p

Identification and molecular characterisation of a fibrinogen binding protein from .-6

Dues.<p><b>Copyright information:</b></p><p>Taken from "Identification and molecular characterisation of a fibrinogen binding protein from ."</p><p>http://www.biomedcentral.com/1471-2180/8/67</p><p>BMC Microbiology 2008;8():67-67.</p><p>Published online 23 Apr 2008</p><p>PMCID:PMC2387161.</p><p></p

Identification and molecular characterisation of a fibrinogen binding protein from .-11

Ansferred to PVDF, then membranes were probed with streptavidin-alkaline phosphatase conjugate and developed with NBT/BCIP. Panel A) Lanes 1 and 2 comprised 5 μl cells grown in vegetable peptone, whilst lanes 2 and 3 contained 5 μl cells grown in barramundi serum. Cells were harvested and washed in TBS before being incubated with biotinylated human fibrinogen (Lanes 1 and 3) or TBS (lanes 2 and 4) for 20 min, prior to extensive washing and transfer onto PVDF membrane for subsequent detection. Fb indicates serial two-fold dilutions of biotinylated fibrinogen commencing at 2.5 μg/mL. Panel B) shows serial 2 × dilutions of 5 μl cells diluted in TBS. Lane F, cells incubated first with TBS then with biotinylated fibrinogen before transfer to the membrane. Lane P+F, cells incubated with barramundi plasma followed by biotinylated fibrinogen, Lane TBS, cells incubated twice in TBS.<p><b>Copyright information:</b></p><p>Taken from "Identification and molecular characterisation of a fibrinogen binding protein from ."</p><p>http://www.biomedcentral.com/1471-2180/8/67</p><p>BMC Microbiology 2008;8():67-67.</p><p>Published online 23 Apr 2008</p><p>PMCID:PMC2387161.</p><p></p

Identification and molecular characterisation of a fibrinogen binding protein from .-9

Ne 3 – QMA0076, lane 4 – QMA0141. A) Transferred lysates stained with Coomassie Brilliant Blue R250. B) Detection of recombinant SiM proteins in lysates with biotinylated fibrinogen.<p><b>Copyright information:</b></p><p>Taken from "Identification and molecular characterisation of a fibrinogen binding protein from ."</p><p>http://www.biomedcentral.com/1471-2180/8/67</p><p>BMC Microbiology 2008;8():67-67.</p><p>Published online 23 Apr 2008</p><p>PMCID:PMC2387161.</p><p></p

Identification and molecular characterisation of a fibrinogen binding protein from .-8

Consensus sequence (after McIver ., 1995).<p><b>Copyright information:</b></p><p>Taken from "Identification and molecular characterisation of a fibrinogen binding protein from ."</p><p>http://www.biomedcentral.com/1471-2180/8/67</p><p>BMC Microbiology 2008;8():67-67.</p><p>Published online 23 Apr 2008</p><p>PMCID:PMC2387161.</p><p></p

Identification and molecular characterisation of a fibrinogen binding protein from .-4

boxes and ribosome binding site – RBS – sequence) are boxed, inverted repeats are highlighted by wedges, the membrane anchor is italicised, the stop codon is bolded and indicated by an asterisk.<p><b>Copyright information:</b></p><p>Taken from "Identification and molecular characterisation of a fibrinogen binding protein from ."</p><p>http://www.biomedcentral.com/1471-2180/8/67</p><p>BMC Microbiology 2008;8():67-67.</p><p>Published online 23 Apr 2008</p><p>PMCID:PMC2387161.</p><p></p

Identification and molecular characterisation of a fibrinogen binding protein from .-10

N, extensively washed and subsequently labelled with FITC-conjugated streptavidin. In each case panel A) indicates bacteria incubated with biotinylated fibrinogen, extensively washed and then stained with streptavidin-FITC under fluorescence, whilst B) is the same field photographed under phase contrast. Panel C) indicates control bacteria, incubated in PBS, extensively washed and stained with streptavidin-FITC to detect any non-specific binding of streptavidin, or autofluorescence whilst D) is the same field observed under phase contrast. For fluorescence microscopy, all fields were exposed manually at ISO800 for 1.3 seconds whilst phase contrast fields were captured using automatic exposure.<p><b>Copyright information:</b></p><p>Taken from "Identification and molecular characterisation of a fibrinogen binding protein from ."</p><p>http://www.biomedcentral.com/1471-2180/8/67</p><p>BMC Microbiology 2008;8():67-67.</p><p>Published online 23 Apr 2008</p><p>PMCID:PMC2387161.</p><p></p

Identification and molecular characterisation of a fibrinogen binding protein from .-0

En, extensively washed and subsequently labelled with FITC-conjugated streptavidin. In each case panel A) indicates bacteria incubated with biotinylated fibrinogen, extensively washed and then stained with streptavidin-FITC under fluorescence, whilst B) is the same field photographed under phase contrast. Panel C) indicates control bacteria, incubated in PBS, extensively washed and stained with streptavidin-FITC to detect any non-specific binding of streptavidin, or autofluorescence whilst D) is the same field observed under phase contrast. For fluorescence microscopy, all fields were exposed manually at ISO800 for 1.3 seconds whilst phase contrast fields were captured using automatic exposure.<p><b>Copyright information:</b></p><p>Taken from "Identification and molecular characterisation of a fibrinogen binding protein from ."</p><p>http://www.biomedcentral.com/1471-2180/8/67</p><p>BMC Microbiology 2008;8():67-67.</p><p>Published online 23 Apr 2008</p><p>PMCID:PMC2387161.</p><p></p

Identification and molecular characterisation of a fibrinogen binding protein from .-3

W. Repeat regions are highlighted. The putative hinge between the two coils is in bold type and the conserved LPXTG membrane anchor near the C-terminal is underlined.<p><b>Copyright information:</b></p><p>Taken from "Identification and molecular characterisation of a fibrinogen binding protein from ."</p><p>http://www.biomedcentral.com/1471-2180/8/67</p><p>BMC Microbiology 2008;8():67-67.</p><p>Published online 23 Apr 2008</p><p>PMCID:PMC2387161.</p><p></p