Open AccessAffinity for porcine respiratory tract mucus is found in some isolates of Actinobacillus pleuropneumoniae
Author(s) -
Bélanger Myriam,
Rioux Stéphane,
Foiry Bernadette,
Jacques Mario
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb05450.x
Subject(s) - actinobacillus pleuropneumoniae , mucus , microbiology and biotechnology , respiratory tract , serotype , biology , pasteurellaceae , dot blot , respiratory system , actinobacillus , bacteria , haemophilus influenzae , biochemistry , anatomy , antibiotics , ecology , dna , genetics
Abstract The ability of 17 Actinobacillus pleuropneumoniae isolates representing serotypes 1, 2, 5, and 7, to adhere in vitro to porcine respiratory tract mucus was examined. Adherence of bacteria to crude mucus preparations was evaluated by use of a dot‐blot assay and an enzyme immunoassay. Seventy per cent (12/17) of the isolates of A. pleuropneumoniae had affinity, to various degress, for porcine respiratory tract mucus. No relationship was found between affinity for respiratory mucus and serotype, haemagglutination, lipopolysaccharide (LPS) profiles, or adherence to porcine tracheal rings. However, a correlation was found between affinity for respiratory mucus and capsular material thickness; heavily encapsulated isolates showed no or less affinity for mucus than isolates with a thinner layer of capsular material. Moreover, two encapsulated isolates showed less affinity for mucus than their acapsulated variant. Finally, the affinity of A . pleuropneumoniae for respiratory mucus was heat‐ and proteinase‐K‐resistant. Our data suggest that capsular material of A. pleuropneumoniae could mask a surface component, possibly LPS, which has affinity for porcine respiratory mucus.