Binding Specificity of Philyra pisum Lectin to Pathogen-Associated Molecular Patterns, and Its Secondary Structure
The Korean Journal of Physiology and Pharmacology
; : 547-551, 2013.
Article
em En
| WPRIM
| ID: wpr-727603
Biblioteca responsável:
WPRO
ABSTRACT
We recently reported a Philyra pisum lectin (PPL) that exerts mitogenic effects on human lymphocytes, and its molecular characterization. The present study provides a more detailed characterization of PPL based on the results from a monosaccharide analysis indicating that PPL is a glycoprotein, and circular dichroism spectra revealing its estimated alpha-helix, beta-sheet, beta-turn, and random coil contents to be 14.0%, 39.6%, 15.8%, and 30.6%, respectively. These contents are quite similar to those of deglycosylated PPL, indicating that glycans do not affect its intact structure. The binding properties to different pathogen-associated molecular patterns were investigated with hemagglutination inhibition assays using lipoteichoic acid from Gram-positive bacteria, lipopolysaccharide from Gram-negative bacteria, and both mannan and beta-1,3-glucan from fungi. PPL binds to lipoteichoic acids and mannan, but not to lipopolysaccharides or beta-1,3-glucan. PPL exerted no significant antiproliferative effects against human breast or bladder cancer cells. These results indicate that PPL is a glycoprotein with a lipoteichoic acid or mannan-binding specificity and which contains low and high proportions of alpha-helix and beta-structures, respectively. These properties are inherent to the innate immune system of P. pisum and indicate that PPL could be involved in signal transmission into Gram-positive bacteria or fungi.
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Índice:
WPRIM
Assunto principal:
Polissacarídeos
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Ácidos Teicoicos
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Neoplasias da Bexiga Urinária
/
Mama
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Glicoproteínas
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Linfócitos
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Lipopolissacarídeos
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Sensibilidade e Especificidade
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Dicroísmo Circular
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Beta-Glucanas
Tipo de estudo:
Diagnostic_studies
Limite:
Humans
Idioma:
En
Revista:
The Korean Journal of Physiology and Pharmacology
Ano de publicação:
2013
Tipo de documento:
Article