Table 1. Alphabetical listing of proven or likely virulence determinants of Bartonella, based on current literature, phenotypes (contact hemolysin, deformin and LPS) and GenBank listings (all others).
Virulence determinant | Bartonella bacilliformis | Bartonella quintana | Bartonella henselae |
---|---|---|---|
BatR/BatS | Present | Present | Present |
Cohemolysin | ? | Present | Present |
Contact hemolysin | Present | Absent | Absent |
C-terminal protease | Present | Present | Present |
Deformin* | Present | ? | ? |
Flagella-mediated motility | Present | Absent | Absent |
Hbp family‡ | Present§ | Present§ | Present§ |
Heme uptake system¶ | Present# | Present | Present |
IalA/IalB** | Present | Present | Present |
LPS with low endotoxicity | Present | Present | Present |
TAAs*‡ | Present | Present | Present |
Trw pilin system | Absent | Present | Present |
VirB/VirD4 and Beps*§ | Absent | Present | Present |
Deformin (deformation factor) has been reported once for Bartonella henselae [13].
Heme-binding proteins. Also referred to as phage-associated protein of 31 kDa (Pap31) of B. henselae.
Three Hbps in Bartonella bacilliformis, five in both B. henselae and Bartonella quintana.
Heme receptor, periplasmic heme-binding protein, ABC transporter/permease and TonB.
A TonB ortholog is not encoded in this genome; possibly uses TolC.
Invasion-associated locus A and B for a nudix hydrolase and erythrocyte invasion protein, respectively.
Trimeric autotransporter adhesins [26]; an orthologous group of YadA-like outer membrane proteins/afimbrial adhesins. Designated as variably-expressed outer membrane proteins in B. quintana, Bartonella repetitive protein A in Bartonella vinsonii, and Bartonella adhesin A in B. henselae.
Type IV secretion system and translocated Beps.
BatR: Bartonella regulator; BatS: Bartonella sensor; Bep: Bartonella effector protein; Hbp: Heme-binding protein; LPS: Lipopolysaccharide; TAA: Trimeric autotransporter adhesin.