Different assembly species of IgM are directed to distinct degradation sites along the secretory pathway.

Rabinovich, Efrat; Bar-Nun, Shoshana; Amitay, Raya; Shachar, Idit; Gür, Burak; Taya, M; Haimovich, Joseph

doi:10.1016/s0021-9258(20)80503-1

Cited by 18 publications

(2 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…4 b). BambL-biotin extracted the mature, fully glycosylated µHC as it is present on the cell surface but not the premature protein of lower molecular weight [ 49 , 50 ]. Similarly, higher Igβ bands were more pronounced in the extract than lower bands.…”

Section: Resultsmentioning

confidence: 99%

Bacterial lectin BambL acts as a B cell superantigen

Frensch

Jäger

Müller

et al. 2021

Cell. Mol. Life Sci.

View full text Add to dashboard Cite

B cell superantigens crosslink conserved domains of B cell receptors (BCRs) and cause dysregulated, polyclonal B cell activation irrespective of normal BCR-antigen complementarity. The cells typically succumb to activation-induced cell death, which can impede the adaptive immune response and favor infection. In the present study, we demonstrate that the fucose-binding lectin of Burkholderia ambifaria, BambL, bears functional resemblance to B cell superantigens. By engaging surface glycans, the bacterial lectin activated human peripheral blood B cells, which manifested in the surface expression of CD69, CD54 and CD86 but became increasingly cytotoxic at higher concentrations. The effects were sensitive to BCR pathway inhibitors and excess fucose, which corroborates a glycan-driven mode of action. Interactome analyses in a model cell line suggest BambL binds directly to glycans of the BCR and regulatory coreceptors. In vitro, BambL triggered BCR signaling and induced CD19 internalization and degradation. Owing to the lectin’s six binding sites, we propose a BCR activation model in which BambL functions as a clustering hub for receptor glycans, modulates normal BCR regulation, and induces cell death through exhaustive activation.

show abstract

Section: Resultsmentioning

confidence: 99%

Bacterial lectin BambL acts as a B cell superantigen

Frensch

Jäger

Müller

et al. 2021

Cell. Mol. Life Sci.

View full text Add to dashboard Cite

show abstract

“…The mHC undergoes glycosylation modification and is transported to the cell surface. The newly synthesized membrane form of mHC is Endo H-resistant, which reaches the cell surface, while the secretory form is Endo H-sensitive (47). Since FUT8 expression is significantly increased during the transition from pro-B to pre-B cell development (8), and since the core fucosylation is required for pre-BCR complex assembly (9), it is conceivable that FUT8 controls the core fucosylation of mHC, followed by pre-BCR complex assembly.…”

Section: Core Fucosylation Regulates Pre-bcr Assemblymentioning

confidence: 99%

Core Fucosylation Regulates the Function of Pre-BCR, BCR and IgG in Humoral Immunity

Sun

Wang

et al. 2022

Front. Immunol.

View full text Add to dashboard Cite

Most of the membrane molecules involved in immune response are glycosylated. N-glycans linked to asparagine (Asn) of immune molecules contribute to the protein conformation, surface expression, stability, and antigenicity. Core fucosylation catalyzed by core fucosyltransferase (FUT8) is the most common post-translational modification. Core fucosylation is essential for evoking a proper immune response, which this review aims to communicate. First, FUT8 deficiency suppressed the interaction between μHC and λ5 during pre-BCR assembly is given. Second, we described the effects of core fucosylation in B cell signal transduction via BCR. Third, we investigated the role of core fucosylation in the interaction between helper T (TH) cells and B cells. Finally, we showed the role of FUT8 on the biological function of IgG. In this review, we discussed recent insights into the sites where core fucosylation is critical for humoral immune responses.

show abstract

TheER–Golgi Membrane System: Compartmental Organization and Protein Traffic

Hauri

Schweizer

1997

Comprehensive Physiology

View full text Add to dashboard Cite

Different assembly species of IgM are directed to distinct degradation sites along the secretory pathway.

Cited by 18 publications

References 24 publications

Bacterial lectin BambL acts as a B cell superantigen

Bacterial lectin BambL acts as a B cell superantigen

Core Fucosylation Regulates the Function of Pre-BCR, BCR and IgG in Humoral Immunity

TheER–Golgi Membrane System: Compartmental Organization and Protein Traffic

Contact Info

Product

Resources

About