No abstract

Summary A polyclonal antibody against the 35 kDa major outer‐membrane protein of Pasteurella multocida cross‐reacted with the 40 kDa major outer‐membrane protein of Actinobacillus pleuropneumoniae and the 42 kDa major outer‐membrane protein of Haemophilus parasuis. The N‐terminal amino‐acid sequences of these proteins revealed a strong homology with the putative 35 kDa porin protein of Pasteurella multocida (66.7 and 76.2%, respectively). Significant homologies were also evident between the 40 kDa and the 42 kDa protein (76.2%), and with non‐specific porins of gram‐negative bacteria.

Outer membrane preparations of various Pasteurella isolates (Pasteurella multocida and some other Pasteurella species) from cattle and swine were extracted by N-lauryl-sarcosine sodium salt. Capsular extracts were prepared by heat treatment. Both preparations bound to epithel cell wall preparations (ECW) of trachea from cattle and to tracheal mucus of cattle and swine. Binding was demonstrated by an enzyme-linked immunosorbent assay (ELISA). Distinct high adherence values were shown by the greater part of membrane preparations of mucoid Pasteurella strains, especially when originating from cattle. U.S.Copyright Clearance CenterCode Statement: 0931 -1793/91/3810-0721$02.50/0 P. rn. nz.