I. Padmalayam et al., THE 75-KILODALTON ANTIGEN OF BARTONELLA-BACILLIFORMIS IS A STRUCTURALHOMOLOG OF THE CELL-DIVISION PROTEIN FTSZ, Journal of bacteriology, 179(14), 1997, pp. 4545-4552
A genomic library of Bartonella bacilliformis was constructed and scre
ened with human anti-Bartonella serum from a patient with the chronic,
verruga peruana phase of bartonellosis. An immunoreactive clone isola
ted from this library was found to code for a 591-amino-acid protein w
ith a high degree of sequence similarity to the FtsZ family of protein
s. The degree of amino acid identity between the B. bacilliformis prot
ein (FtsZ(Bb)) and the other FtsZ proteins is especially pronounced ov
er the N-terminal 321 amino acids (N-terminal domain) of the sequence,
with values ranging from 45% identity for the homolog from Micrococcu
s luteus (FtsZMl) to 91% identity for the homolog from Rhizobium melli
loti, (FtsZ(Rm1)). All of the functional domains required for FtsZ act
ivity are conserved in FtsZ(Bb) and are located within the N-terminal
domain of the protein. FtsZ(Bb) is approximately twice as large as mos
t of the other FtsZ proteins previously reported, a property it shares
with FtsZ(Rm1). Like the Rhizobium homolog, FtsZ(Bb) has a C-terminal
region of approximately 256 amino acids that is absent in the other F
tsZ proteins. Evidence is presented that implicates this region in the
protein's antigenicity and suggests that, unlike most other FtsZ homo
logs, FtsZ(Bb) is at least partly exposed at the cell surface. PCR ana
lysis revealed that an ftsZ gene similar in size to the B. bacilliform
is gene is present in Bartonella henselae, a bacterium that is closely
related to B. bacilliformis.