Characterization of outer membrane and secreted proteins of Leptospira interrogans serovar pomona.

Abstract:

:Outer membrane and secreted proteins were isolated from Leptospira interrogans serovar pomona and characterized by sodium dodecyl sulfate polyacrylamide gel electrophoresis, immunoblot and radioimmunoprecipitation techniques. The L. interrogans outer membranes were extracted with Triton X-114 and contained several proteins. The major cellular protein with a molecular mass of 31 kDa was associated exclusively with the L. interrogans outer membrane. Using a whole cell immunoprecipitation method, five hydrophobic, Triton X-114 extractable proteins (22, 26, 31, 36 and 42 kDa) were exposed on the surface of L. interrogans. The 31 kDa protein was heat labile and was a potent antigen in animals experimentally infected with L. interrogans serovar pomona. Several proteins were secreted by L. interrogans including a 60 kDa protein tentatively identified as the L. interrogans hemolysin.

journal_name

Microb Pathog

journal_title

Microbial pathogenesis

authors

Zuerner RL,Knudtson W,Bolin CA,Trueba G

doi

10.1016/0882-4010(91)90014-2

subject

Has Abstract

pub_date

1991-04-01 00:00:00

pages

311-22

issue

4

eissn

0882-4010

issn

1096-1208

pii

0882-4010(91)90014-2

journal_volume

10

pub_type

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