Mucosal Immunology 2015
DOI: 10.1016/b978-0-12-415847-4.00022-7
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Microbial Evasion of IgA Functions

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Cited by 12 publications
(7 citation statements)
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“…Although the Faba fragments may still coat the organisms through recognition of specific antigens, the loss of the Fc region renders them unable to trigger effector mechanisms. Moreover, they prevent recognition of the organism by intact antibodies of other isotypes, thereby allowing the bacterium to evade the protective functions of mucosal Igs (180).…”
Section: Iga1 Proteasesmentioning
confidence: 99%
“…Although the Faba fragments may still coat the organisms through recognition of specific antigens, the loss of the Fc region renders them unable to trigger effector mechanisms. Moreover, they prevent recognition of the organism by intact antibodies of other isotypes, thereby allowing the bacterium to evade the protective functions of mucosal Igs (180).…”
Section: Iga1 Proteasesmentioning
confidence: 99%
“…The molecular basis for the host specificity of pathogenic Neisseria is not fully understood, but the existing evidence indicates that multiple factors are involved. On the pathogen side, a number of surface-exposed proteins appear to be associated with the human specificity of pathogenic Neisseria , including immunoglobulin A1 (IgA1) protease, 12 , 13 type IV pili, 14 , 15 , 16 complement factor H binding proteins (FHBP), 17 , 18 gonococcal porin, 19 transferrin-binding proteins 20 , 21 and lactoferrin-binding proteins. 21 , 22 On the host side, several human proteins have been implicated as host specificity determinants, including IgA1, 12 , 13 cell surface complement regulator CD46, 10 complement regulator factor H (FH), 17 , 18 , 23 complement regulator C4b-binding protein (C4BP), 19 transferrin 9 , 24 , 25 and lactoferrin.…”
Section: Human-specific Pathogensmentioning
confidence: 99%
“…As illustrated in Figure 1 , N. gonorrhoeae and N. meningitidis produce an extracellular serine-type protease that specifically cleaves human IgA1, a subclass of the dominant mucosal antibody, IgA. 12 , 13 IgA1 is the most abundant antibody in upper respiratory secretions. 26 IgA serves as a ‘non-inflammatory mucosal protector' at mucosal surfaces, performing multiple important functions, such as inhibition of microbial adherence, neutralization of microorganisms and inhibition of antigen penetration.…”
Section: Human-specific Pathogensmentioning
confidence: 99%
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“…Salivary s-IgA inhibits microbial colonization and neutralizes microbial enzymes or toxins [ 56–58 ]. Salivary s-IgA antibody can prevent the colonization of Streptococcus mutans by neutralizing glycosyltransferase (GTF), thus reducing the rate of GTF binding to Streptococcus mutans pili, thus inhibiting the development of dental caries [ 59 , 60 ]. Another potential mechanism is that salivary s-IgA can synergize and promote the bacteriostasis of the lactoferrin and peroxidase system, which can also explain the correlation between salivary s-IgA and caries [ 61–63 ].…”
Section: Discussionmentioning
confidence: 99%