Arylneuraminidase activity of Pseudomonas aeruginosa does not degrade natural substrates such as human respiratory mucins.
The culture supernatant from a single Pseudomonas aeruginosa strain has been reported to show neuraminidase activity, leading to the speculation that this bacterium may use this enzyme as a virulence factor to act on host macromolecules. In order to extend this finding, we have examined the activity of concentrated P. aeruginosa culture supernatants and cells on synthetic and natural substrates containing sialic acid, such as human respiratory mucins. Four P. aeruginosa strains showed some activity on the synthetic substrate 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid but failed to liberate N-acetylneuraminic acid from six different natural substrates. Attempts to induce enzyme production by use of human respiratory mucins in the culture medium were also unsuccessful. The supernatants also showed N-acetyl-beta-D-glucosaminidase-like activity on a synthetic substrate but did not liberate N-acetylhexosamines from natural substrates. We conclude that the neuraminidase-like activity observed in P. aeruginosa can be defined as an arylneuraminidase and that the possession of a neuraminidase active on natural substrates is not a common attribute of P. aeruginosa strains.
Unité Institute National de la Santé et de la Recherche Médicale, Lille, France.
A
A
Scharfman
R
R
Ramphal
C
C
Neut
C
C
Carnoy
G
G
Lamblin
P
P
Roussel
D005110:Extracellular Space / Q000201:enzymology; D009077:Mucins / Q000378:metabolism*; D019158:N-Acetylneuraminic Acid; D009439:Neuraminidase / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D012794:Sialic Acids / Q000378:metabolism; D012795:Sialoglycoproteins / Q000378:metabolism; D013379:Substrate Specificity
D009077:Mucins; D012794:Sialic Acids; D012795:Sialoglycoproteins; D009439:Neuraminidase; D019158:N-Acetylneuraminic Acid