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VF category: Biofilm formation (total 233 related VFs in database, current show from 121 to 130)
 
VF Bacteria Brief description
Agf
(Thin aggregative fimbriae (or curli))
Salmonella
(S. enterica subsp. enterica serovar Paratyphi C strain RKS4594)
Homology to csg of E.coli. Nucleator-dependent assembly pathway. Aids in attachment to the villi of enterocytes, also cause the bacteria to become attached to each other. ...
Agf
(Thin aggregative fimbriae (or curli))
Salmonella
(S. enterica subsp. enterica serovar Schwarzengrund str. CVM19633)
Homology to csg of E.coli. Nucleator-dependent assembly pathway. Aids in attachment to the villi of enterocytes, also cause the bacteria to become attached to each other. ...
Agf
(Thin aggregative fimbriae (or curli))
Salmonella
(S. enterica subsp. enterica serovar Typhi str. CT18)
Homology to csg of E.coli. Nucleator-dependent assembly pathway. Aids in attachment to the villi of enterocytes, also cause the bacteria to become attached to each other. ...
Agf
(Thin aggregative fimbriae (or curli))
Salmonella
(S. enterica subsp. enterica serovar Typhi str. Ty2)
Homology to csg of E.coli. Nucleator-dependent assembly pathway. Aids in attachment to the villi of enterocytes, also cause the bacteria to become attached to each other. ...
BapA
(Biofilm-associated protein)
Salmonella
(S. enterica subsp. enterica serovar Typhimurium str. LT2)
Biofilm-associated proteins (BAPs) are important for early biofilm formation (adhesion) by bacteria and are also found in mature biofilms. BAPs were first reported in Staphylococcus aureus and proteins that have homology to these are termed BAPs. BAPs are conserved across the bacterial kingdom, in proteins such as Mus-20 (Pseudomonas putida), BapA (Salmonella enteritidis), Bap (Burkholderia cepacia), Espfm (Enterococcus faecium), Esp (Enterococcus faecalis), and LapA (Pseudomonas fluorescens). The T1SS-secreted adhesin BapA is encoded by a gene within Salmonella Pathogenicity Island SPI9. ...
IcsA (VirG)
(Ics for intercellular spread)
Shigella
(S. boydii CDC 3083-94)
Three distinctive domains: the N-terminal signal sequence (1-52), the 706 α-domain (53-758), the 344 C-terminal β-core. β-core embedded in the outer membrane, the C-terminal ~220 aa of IcsAα (509-729) are essential for the unipolar distribution of IcsA, the residues (103-433) are the binding site for N-WASP. residues (53-506) is the region of vinculin interaction and is essential for F-actin assembly. ...
IcsA (VirG)
(Ics for intercellular spread)
Shigella
(S. dysenteriae Sd197)
Three distinctive domains: the N-terminal signal sequence (1-52), the 706 α-domain (53-758), the 344 C-terminal β-core. β-core embedded in the outer membrane, the C-terminal ~220 aa of IcsAα (509-729) are essential for the unipolar distribution of IcsA, the residues (103-433) are the binding site for N-WASP. residues (53-506) is the region of vinculin interaction and is essential for F-actin assembly. ...
IcsA (VirG)
(Ics for intercellular spread)
Shigella
(S. sonnei Ss046)
Three distinctive domains: the N-terminal signal sequence (1-52), the 706 α-domain (53-758), the 344 C-terminal β-core. β-core embedded in the outer membrane, the C-terminal ~220 aa of IcsAα (509-729) are essential for the unipolar distribution of IcsA, the residues (103-433) are the binding site for N-WASP. residues (53-506) is the region of vinculin interaction and is essential for F-actin assembly. ...
IcsA (VirG)
(Ics for intercellular spread)
Shigella
(S. flexneri 5a str. M90T)
Three distinctive domains: the N-terminal signal sequence (1-52), the 706 α-domain (53-758), the 344 C-terminal β-core. β-core embedded in the outer membrane, the C-terminal ~220 aa of IcsAα (509-729) are essential for the unipolar distribution of IcsA, the residues (103-433) are the binding site for N-WASP. residues (53-506) is the region of vinculin interaction and is essential for F-actin assembly. ...
Intercellular adhesion proteins
Staphylococcus
(S. aureus RF122)
icaA, icaB, icaC, icaD synthesize a polysaccharide, poly-n-succinyl-β-1,6 glucosamine (PNSG) during infection. ...
   


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