Purpose: A major component of bladder surface mucin is a glycoprotein GP51
(molecular weight 51 kD.). GP51, which has previously been isolated from ra
bbit mucosa, appears to function as part of the defense mechanism in an in
vivo infection model. GP51 coats the epithelium and is secreted into the ur
ine, as detected by immunohistochemical testing and enzyme-linked immunosor
bent assay (ELISA). Increased urinary GP51 occurs during urinary tract infe
ction. To elucidate the role of GP51 as a component of the primary defense
mechanism we studied interactions with uropathogenic bacterial isolates and
urine from symptomatic patients with urinary tract infection.
Materials and Methods: ELISA was performed to demonstrate the binding of GP
51 and various uropathogens. Immunochemical studies were done using monoclo
nal antibodies to GP51 to determine the interaction of GP51 with certain ur
opathogenic isolates, including Escherichia coli, Enterobacter cloacae, Kle
bsiella pneumoniae, Proteus vulgaris, Pseudomonas aeruginosa, Serratia marc
escens, Staphylococcus aureus, S. epidermidis and Streptococcus faecalis. I
nfected urinary sediments and uropathogenic bacterial cultures were examine
d by immunocytochemical testing to localize GP51. Antigen inhibition ELISA
was done to quantitate urinary GP51 in the urine of 17 normal controls and
19 patients with urinary tract infection.
Results: ELISA revealed that GP51 binds to a wide spectrum of gram-positive
and gramnegative uropathogens in semiquantitative fashion. Immunochemical
methods confirmed that purified GP51 binds to bacteria, encapsulating and a
ggregating the bacteria. Clinical specimens showed GP51 localized to bacter
ia and uroepithelial cells. We observed a significant increase in urinary G
P51 in urinary tract infection compared to uninfected urine (p = 0.0003).
Conclusions: These studies suggest that GP51, a component of bladder mucin,
may be a strategic factor in the primary defense mechanism of the bladder.