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Literature summary for 3.4.24.13 extracted from

  • Fasching, C.E.; Grossman, T.; Corthesy, B.; Plaut, A.G.; Weiser, J.N.; Janoff, E.N.
    Impact of the molecular form of immunoglobulin A on functional activity in defense against Streptococcus pneumoniae (2007), Infect. Immun., 75, 1801-1810.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed as a His-tagged Haemophilus influenzae type 1 IgA1 protease Haemophilus influenzae

Protein Variants

Protein Variants Comment Organism
additional information polymeric IgA and secretory IgA are tested for killing of an IgA1 protease producing strain and a congenic IgA1 protease-negative strain of Streptococcus pneumoniae after a 2 h bacterium-antibody exposure time. Exposure of polymeric IgA and secretory IgA to the protease-producing strain inhibits IgA-mediated killing compared with the results seen with polymeric IgA and secretory IgA exposed to a protease-negative mutant. No difference in killing is observed between the two bacterial strains when polymeric IgA and secretory IgA of subclass IgA2 are used Streptococcus pneumoniae

Organism

Organism UniProt Comment Textmining
Haemophilus influenzae
-
-
-
Streptococcus pneumoniae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using Ni-NTA agorose binding Haemophilus influenzae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
human monoclonal capsule-specific IgA + H2O
-
Haemophilus influenzae ?
-
?
additional information all three forms of capsule-specific IgA show comparable susceptibilities to cleavage by bacterial IgA1 protease, demonstrating that secretory component does not prevent the proteolytic degradation of IgA1 by IgA1 protease. IgA1 cleavage results in formation of identical Fab fragments for each of the molecular forms, thereby abolishing the contribution of multivalence of polymeric IgA and secretory IgA Haemophilus influenzae ?
-
?
additional information polymeric and secretory IgA show comparable susceptibilities to functional inhibition by bacterial IgA1 protease cleavage, demonstrating that secretory component does not prevent the proteolytic degradation of IgA1 by IgA1 protease Streptococcus pneumoniae ?
-
?
polymeric IgA + H2O
-
Haemophilus influenzae ?
-
?
polymeric IgA + H2O
-
Streptococcus pneumoniae ?
-
?
secretory IgA + H2O
-
Haemophilus influenzae ?
-
?
secretory IgA + H2O
-
Streptococcus pneumoniae ?
-
?

Synonyms

Synonyms Comment Organism
IgA1 protease
-
Haemophilus influenzae
IgA1 protease
-
Streptococcus pneumoniae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Haemophilus influenzae
37
-
assay at Streptococcus pneumoniae