Defense mechanisms involving Fc-dependent functions of immunoglobulin A and their subversion by bacterial immunoglobulin A proteases.

Kilian, Mogens; Městecký, Jiří; Russell, Michael W.

doi:10.1128/mmbr.52.2.296-303.1988

Cited by 211 publications

(138 citation statements)

References 43 publications

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“…Functional differences between the IgA subclasses are beginning to be revealed. IgA2 is resistant to IgA1 proteases produced by several pathogenic bacteria, including Haemophilus influenzae type b (Hib), Streptococcus pneumoniae and Neisseria meningitidis [12,13]. Hence, high concentrations of specific IgA2 on the mucosa may be beneficial in defence against these pathogens.…”

Section: Introductionmentioning

confidence: 99%

Subclass distribution of IgA antibodies in saliva and serum after immunization withHaemophilus influenzaetype b conjugate vaccines

Kauppi-Korkeila

Saarinen

Eskola

et al. 1998

Clinical and Experimental Immunology

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SUMMARYIgA subclass distribution of antibodies against capsular polysaccharide (PS) of Haemophilus influenzae type b (Hib) was studied in saliva and serum samples of children vaccinated with two (n ¼ 58) or three doses (n ¼ 53) of Hib vaccine. One month after the second dose of Hib conjugate vaccine, at 7 months old, 40% of the children had IgA1 and 41% had IgA2 anti-Hib PS antibodies in saliva. One month after the third dose, at 15-25 months old, IgA1 was the predominating subclass; 72% of the children had IgA1, 26% had IgA2 anti-Hib PS in saliva. The mean concentration of IgA1 anti-Hib PS, expressed as optical density (OD) values, was significantly higher after three doses (OD 80·7) than after two doses (OD 18·9). The mean concentration of IgA2 did not change significantly after the third dose (OD 23·8 after two doses, OD 18·1 after three doses). In serum, IgA1 anti-Hib PS predominated both after two (17% had IgA1, none had IgA2) and three doses (72% had IgA1, 4% had IgA2) of Hib vaccine. In conclusion, both IgA1 and IgA2 anti-Hib PS were found in saliva of immunized children after two doses of Hib conjugate vaccine, whereas the third vaccine dose induced a shift towards IgA1 anti-Hib PS dominance in saliva.

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Section: Introductionmentioning

confidence: 99%

Subclass distribution of IgA antibodies in saliva and serum after immunization withHaemophilus influenzaetype b conjugate vaccines

Kauppi-Korkeila

Saarinen

Eskola

et al. 1998

Clinical and Experimental Immunology

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“…Exogenous steroids. Bauer et al,9~ in a large multicentered collaborative randomized tiral, found a significantly decreased (p = 0.002) incidence of NEC in the infants whose mothers had been treated with steroids antenatally. Accelerated intestinal maturation induced by antenatal maternal steroid therapy may have accounted for the decreased incidence of NEC in steroid-exposed infants.…”

Section: Volume 117mentioning

confidence: 97%

Gastrointestinal host defense and necrotizing enterocolitis

Udall¹

1990

The Journal of Pediatrics

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“…103 6SHFL¿F,J$ SURWHDVH DFWLYLW\ LV D ZHOOHVWDEOLVKHG IHDWXUH RI PDQ\ KXPDQ LQIHFWLRXV diseases that take place at, or originate from, mucosal surfaces. 105,106 For bacterial pathogens WKH ,J$ SURWHDVHV KDYH EHHQ SULPDULO\ FODVVL¿HG DV VHULQH RU PHWDOORW\SH SURWHDVHV cleaving only the IgAl subclass of antibody, because the susceptible site is one of the Pro-Ser or Pro-Thr peptide bonds located within a 12-amino acid proline rich sequence in the hinge region of IgAl but absent from IgA2. 106,107 However, the cathepsin B-like cysteine protease (EhCp5) secreted by the protozoan E. histolytica with a preference for Arg-Arg residues displays an ability to cleave both IgA1 and IgA2 degrading the antibody structures at positions 245 and 250 of the hinge region.…”

Section: Degradation Of Immunoglobulinsmentioning

confidence: 99%

“…105,106 For bacterial pathogens WKH ,J$ SURWHDVHV KDYH EHHQ SULPDULO\ FODVVL¿HG DV VHULQH RU PHWDOORW\SH SURWHDVHV cleaving only the IgAl subclass of antibody, because the susceptible site is one of the Pro-Ser or Pro-Thr peptide bonds located within a 12-amino acid proline rich sequence in the hinge region of IgAl but absent from IgA2. 106,107 However, the cathepsin B-like cysteine protease (EhCp5) secreted by the protozoan E. histolytica with a preference for Arg-Arg residues displays an ability to cleave both IgA1 and IgA2 degrading the antibody structures at positions 245 and 250 of the hinge region. 108,109 Similar to the proteolytic cleavage of IgG described above, release of Fab fragments inhibits antigen disposal as immunogenic determinants are masked by fabulation.…”

Section: Degradation Of Immunoglobulinsmentioning

confidence: 99%

How Pathogen-Derived Cysteine Proteases Modulate Host Immune Responses

Donnelly

Dalton

Robinson

2011

Advances in Experimental Medicine and Biology

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In mammals, cysteine proteases are essential for the induction and development of both innate and adaptive immune responses. These proteases play a role in antigen-and pathogen-recognition and elimination, signal processing and cell homeostasis. Many pathogens also secrete cysteine proteases that often act on the same target proteins as the mammalian proteases and thereby can modulate host immunity from initial recognition to effector mechanisms. Pathogen-derived proteases range from nonspecific proteases that degrade multiple proteins involved in the immune response to enzymes that are very specific in their mode of action. Here, we overview current knowledge of pathogen-derived cysteine proteases that modulate immune responses by altering the normal function of key receptors or pathways in the mammalian immune system.

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Defense mechanisms involving Fc-dependent functions of immunoglobulin A and their subversion by bacterial immunoglobulin A proteases.

Cited by 211 publications

References 43 publications

Subclass distribution of IgA antibodies in saliva and serum after immunization withHaemophilus influenzaetype b conjugate vaccines

Subclass distribution of IgA antibodies in saliva and serum after immunization withHaemophilus influenzaetype b conjugate vaccines

Gastrointestinal host defense and necrotizing enterocolitis

How Pathogen-Derived Cysteine Proteases Modulate Host Immune Responses

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