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Borrelia burgdorferi, the causative agent of
Lyme disease, undergoes a loss in virulence with repeated passage in vitro. Defining the changes which occur after conversion to avirulence may assist in identifying virulence factors and mechanisms of pathogenesis. We have used a cross-adsorption technique and two-dimensional nonequilibrium pH gradient electrophoresis to compare virulent (low-passage) and avirulent (high-passage) variants of B. Burgdorferi B31. Using cross-adsorbed rabbit sera to probe immunoblots, we identified 10 low-passage-associated proteins (relative molecular masses of 78, 58, 49, 34, 33, 28, 24, 20, and 16 kDa) unique to the virulent strain B31. Cross-adsorbed human serum detected five proteins of similar sizes (78, 58, 34, 28, and 20 kDa), suggesting that several of of these proteins were expressed during human infection. By probing inner and outer membranes, two proteins (58 and 33 kDa) that localized specifically to the outer membrane were observed. An additional low-passage-associated protein (28 kDa) was identified when outer membranes from low- and high-pressure variants of strain B31 were compared by two-dimensional nonequilibrium pH gradient electrophoresis.