M. Cedzynski et al., STRUCTURAL AND SEROLOGICAL STUDIES OF THE O-ANTIGEN OF THE BACTERIUM PROTEUS-VULGARIS OX2 (SEROGROUP O2) USED IN THE WEIL-FELIX TEST, Biochemistry, 62(1), 1997, pp. 15-20
Based on monosaccharide analysis and H-1- and C-13-NMR spectroscopy, t
he following structure of the O-specific polysaccharide chain of Prote
us vulgaris OX2 lipopoiysaccharide (LPS), which defines the O2 specifi
city of Proteus, was established: [GRAPHICS] where L-QuiNAc is N-acety
l-L-quinovosamine (2-acetamido-2,6-dideoxy-L-glucose). Various strains
of P. vulgaris OX2 used in the Weil-Felix test for serodiagnosis of r
ickettsiosis (spotted fevers, except for Rocky Mountain spotted fever)
were shown to produce LPS with the same O-specific polysaccharide, wh
ich differs structurally and serologically from LPS of P. vulgaris OX1
9 used as antigen for serodiagnosis of typhus and Rocky Mountain spott
ed fever. O-Acetyl groups present in the polysaccharide are not import
ant for manifesting the immunospecificity. ELISA confirmed that the ep
itope responsible for the cross-reactivity between sera from patients
with Japanese spotted fever and P. vulgaris OX2 cells is located on th
e P. vulgaris LPS. At the same time, no cross-reaction was observed be
tween rabbit anti-P. vulgaris OX2 antibodies and the spotted fever gro
up (SFG) rickettsial cells. Therefore, human anti-SFG rickettsial anti
bodies and rabbit anti-P, vulgaris OX2 antibodies may bind to distinct
epitopes on P. vulgaris OX2 LPS, and no epitope recognized by rabbit
anti-P. vulgaris OX2 antibodies is present on the LPS or any other sur
face antigen of SFG rickettsiae.