Sandbox Reserved 818: Difference between revisions

Line 24:

==Binding of pertussis toxin to its cellular targets==

After being secreted, pertussis toxin (PTX) can interact with almost all mammalian cells, which explains the variety of biological activities of the toxin.

No specific receptors for PTX have been identified but many cell surface '''sialoglycoproteins''' are involved in the binding of PTX, together with '''glycoproteins''': sugar moieties allow the recognition of the toxin and the carbohydrate sequence '''NeuAcα(2,6)-Galβ4GlcNAc''' is particularly important but sugar sequence alone is not sufficient.

No specific receptors for PTX have been identified but many cell surface '''sialoglycoproteins''' are involved in the binding of PTX [64], together with '''glycoproteins''': sugar moieties allow the recognition of the toxin and the carbohydrate sequence '''NeuAcα(2,6)-Galβ4GlcNAc''' is particularly important but sugar sequence alone is not sufficient [69].

PTX binds its target cells through the ''B oligomer'' : ''S2'' and ''S3'' subunits contains at least two '''carbohydrate-binding sites'''. The N-terminal regions of these subunits are involved in receptor binding and the C-terminal domains of S2 and S3 adopt a fold found in other carbohydrate-binding proteins.

PTX binds its target cells through the ''B oligomer'' : ''S2'' and ''S3'' subunits contains at least two '''carbohydrate-binding sites''' [70]. The N-terminal regions of these subunits are involved in receptor binding and the C-terminal domains of S2 and S3 adopt a fold found in other carbohydrate-binding proteins [73].

The B oligomer of PTX is involved in some biological activities of the toxin, independently of the enzyme activity. Thus '''Asn105''' in ''S2'' and '''Lys103''' in ''S3'' are important for the mitogenic activity of pertussis toxin on murine T lymphocytes, but not on human T cells.

The B oligomer of PTX is involved in some biological activities of the toxin, independently of the enzyme activity. Thus '''Asn105''' in ''S2'' and '''Lys103''' in ''S3'' are important for the mitogenic activity of pertussis toxin on murine T lymphocytes [71], but not on human T cells [74].

==Toxin entry and trafficking in target cells==

Sandbox Reserved 818: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 24: / Line 24: @@
 ==Binding of pertussis toxin to its cellular targets==
 After being secreted, pertussis toxin (PTX) can interact with almost all mammalian cells, which explains the variety of biological activities of the toxin. <br />
-No specific receptors for PTX have been identified but many cell surface '''sialoglycoproteins''' are involved in the binding of PTX, together with '''glycoproteins''': sugar moieties allow the recognition of the toxin and the carbohydrate sequence '''NeuAcα(2,6)-Galβ4GlcNAc''' is particularly important but sugar sequence alone is not sufficient. <br />
+No specific receptors for PTX have been identified but many cell surface '''sialoglycoproteins''' are involved in the binding of PTX [64], together with '''glycoproteins''': sugar moieties allow the recognition of the toxin and the carbohydrate sequence '''NeuAcα(2,6)-Galβ4GlcNAc''' is particularly important but sugar sequence alone is not sufficient [69]. <br />
-PTX binds its target cells through the ''B oligomer'' : ''S2'' and ''S3'' subunits contains at least two '''carbohydrate-binding sites'''. The N-terminal regions of these subunits are involved in receptor binding and the C-terminal domains of S2 and S3 adopt a fold found in other carbohydrate-binding proteins. <br />
+PTX binds its target cells through the ''B oligomer'' : ''S2'' and ''S3'' subunits contains at least two '''carbohydrate-binding sites''' [70]. The N-terminal regions of these subunits are involved in receptor binding and the C-terminal domains of S2 and S3 adopt a fold found in other carbohydrate-binding proteins [73]. <br />
-The B oligomer of PTX is involved in some biological activities of the toxin, independently of the enzyme activity. Thus '''Asn105''' in ''S2'' and '''Lys103''' in ''S3'' are important for the mitogenic activity of pertussis toxin on murine T lymphocytes, but not on human T cells.
+The B oligomer of PTX is involved in some biological activities of the toxin, independently of the enzyme activity. Thus '''Asn105''' in ''S2'' and '''Lys103''' in ''S3'' are important for the mitogenic activity of pertussis toxin on murine T lymphocytes [71], but not on human T cells [74].
 ==Toxin entry and trafficking in target cells==