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<i>Brucella</i>sp. bind to sialic acid residues on human and animal red blood cells
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Citations
24
References
2002
Year
ImmunohematologyImmunologyBlood CellCell DeathPathologySialic Acid ResiduesImmune SystemHeme TraffickingHematologyBrucella AbortusHealth SciencesBiochemistryGranulocyteHeme SignalingRabbit Anti-sp29 AntibodiesMetalloproteinPathogenesis29-Kda Surface ProteinMicrobiologyMedicine
We report that Brucella abortus and Brucella melitensis agglutinate human (A+ and B+), hamster and rabbit erythrocytes, a heretofore undescribed feature in this genus. This activity was associated with a 29-kDa surface protein (SP29) that bound selectively to these erythrocytes and this binding was inhibited by rabbit anti-SP29 antibodies. Hemagglutination was inhibited by pretreatment of erythrocytes with neuraminidase and by preincubation of B. abortus with chondroitin sulfate, N-acetylneuraminic acid and N-acetylneuramin-lactose.
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