Faculty Opinions recommendation of Recognition of DHN-melanin by a C-type lectin receptor is required for immunity to Aspergillus.

AbstractSemen is important in determining HIV-1 susceptibility but it is unclear how it affects virus transmission during sexual contact. Mucosal Langerhans cells (LCs) are the first immune cells to encounter HIV-1 during sexual contact and have a barrier function as LCs are restrictive to HIV-1. As semen from people living with HIV-1 contains complement-opsonized HIV-1, we investigated the effect of complement on HIV-1 dissemination by human LCs in vitro and ex vivo. Notably, pre-treatment of HIV-1 with semen enhanced LC infection compared to untreated HIV-1 in the ex vivo explant model. Infection of LCs and transmission to target cells by opsonized HIV-1 was efficiently inhibited by blocking complement receptors CR3 and CR4. Complement opsonization of HIV-1 enhanced uptake, fusion, and integration by LCs leading to an increased transmission of HIV-1 to target cells. However, in the absence of both CR3 and CR4, C-type lectin receptor langerin was able to restrict infection of complement-opsonized HIV-1. These data suggest that complement enhances HIV-1 infection of LCs by binding CR3 and CR4, thereby bypassing langerin and changing the restrictive nature of LCs into virus-disseminating cells. Targeting complement factors might be effective in preventing HIV-1 transmission.

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Corrigendum to selective expression of a C-type lectin receptor, Clec12b, on skin mast cells

Biochemical and Biophysical Research Communications ◽

10.1016/j.bbrc.2021.07.009 ◽

2021 ◽

Author(s):

Ayana Iijima ◽

Kazumasa Kanemaru ◽

Yaqiu Wang ◽

Tsukasa Nabekura ◽

Yoshiyuki Nakamura ◽

...

Keyword(s):

Mast Cells ◽

Lectin Receptor ◽

Selective Expression

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Cytological Observation and Transcriptome Comparative Analysis of Self-Pollination and Cross-Pollination in Dendrobium Officinale

Genes ◽

10.3390/genes12030432 ◽

2021 ◽

Vol 12 (3) ◽

pp. 432

Author(s):

Yaling Chen ◽

Benchang Hu ◽

Fantao Zhang ◽

Xiangdong Luo ◽

Jiankun Xie

Keyword(s):

Pollen Tubes ◽

The Self ◽

Dendrobium Officinale ◽

Self Incompatibility ◽

Related Gene ◽

Cytological Observation ◽

Lectin Receptor ◽

Cross Pollination ◽

Self Pollination ◽

Medicinal Value

Dendrobium officinale is a rare and traditional medicinal plant with high pharmacological and nutritional value. The self-incompatibility mechanism of D. officinale reproductive isolation was formed in the long-term evolution process, but intraspecific hybridization of different germplasm resources leads to a large gap in the yield, quality, and medicinal value of D. officinale. To investigate the biological mechanism of self-incompatibility in D. officinale, cytological observation and the transcriptome analysis was carried out on the samples of self-pollination and cross-pollination in D. officinale. Results for self-pollination showed that the pollen tubes could grow in the style at 2 h, but most of pollen tubes stopped growing at 4 h, while a large number of cross-pollinated pollen tubes grew along the placental space to the base of ovary, indicating that the self-incompatibility of D. officinale may be gametophyte self-incompatibility. A total of 63.41 G basesum of D. officinale style samples from non-pollinated, self-pollination, and cross-pollination by RNA-seq were obtained, and a total of 1944, 1758, and 475 differentially expressed genes (DEGs) in the comparison of CK (non-pollinated) vs. HF (cross-pollination sample), CK vs. SF (self-pollination sample) and SF vs. HF were identified, respectively. Forty-one candidate genes related to self-incompatibility were found by function annotation of DEGs, including 6 Ca2+ signal genes, 4 armed repeat containing (ARC) related genes, 11 S-locus receptor kinase (SRK) related genes, 2 Exo70 family genes, 9 ubiquitin related genes, 1 fatty acid related gene, 6 amino acid-related genes, 1 pollen-specific leucine-rich repeat extensin-like protein (LRX) related gene and 1 lectin receptor-like kinases (RLKs) related gene, showed that self-incompatibility mechanism of D. officinale involves the interaction of multiple genes and pathways. The results can provide a basis for the study of the self-incompatibility mechanism of D. officinale, and provide ideas for the preservation and utilization of high-quality resources of D. officinale.

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Ambiguity about Splicing Factor 3b Subunit 3 (SF3B3) and Sin3A Associated Protein 130 (SAP130)

Cells ◽

10.3390/cells10030590 ◽

2021 ◽

Vol 10 (3) ◽

pp. 590

Author(s):

Paula I. Metselaar ◽

Celine Hos ◽

Olaf Welting ◽

Jos A. Bosch ◽

Aletta D. Kraneveld ◽

...

Keyword(s):

Immune System ◽

Histone Deacetylase ◽

Mendelian Inheritance ◽

Splicing Factor ◽

Online Mendelian Inheritance ◽

Lectin Receptor ◽

Corepressor Complex ◽

A Subunit

In 2020, three articles were published on a protein that can activate the immune system by binding to macrophage-inducible C-type lectin receptor (Mincle). In the articles, the protein was referred to as ‘SAP130, a subunit of the histone deacetylase complex.’ However, the Mincle ligand the authors aimed to investigate is splicing factor 3b subunit 3 (SF3B3). This splicing factor is unrelated to SAP130 (Sin3A associated protein 130, a subunit of the histone deacetylase-dependent Sin3A corepressor complex). The conclusions in the three articles were formulated for SF3B3, while the researchers used qPCR primers and antibodies against SAP130. We retraced the origins of the ambiguity about the two proteins and found that Online Mendelian Inheritance in Man (OMIM) added a Nature publication on SF3B3 as a reference for Sin3A associated protein 130 in 2016. Subsequently, companies such as Abcam referred to OMIM and the Nature article in their products for both SF3B3 and SAP130. In turn, the mistake by OMIM followed in the persistent and confusing use of ‘SAP130′ (spliceosome-associated protein 130) as an alternative symbol for SF3B3. With this report, we aim to eliminate the persistent confusion and separate the literature regarding the two proteins.

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Effect of polyvalencies of glycotopes on the binding of a lectin from the edible mushroom, Agaricus bisporus

Biochemical Journal ◽

10.1042/bj20021361 ◽

2003 ◽

Vol 371 (2) ◽

pp. 311-320 ◽

Cited By ~ 40

Author(s):

Albert M. WU ◽

June H. WU ◽

Anthony HERP ◽

Jia-Hau LIU

Keyword(s):

Agaricus Bisporus ◽

Therapeutic Potential ◽

Specific Binding ◽

Biological Activities ◽

Edible Mushroom ◽

Structural Requirement ◽

Colon Cells ◽

Lectin Receptor ◽

Proliferative Effect ◽

Potent Factor

Agaricus bisporus agglutinin (ABA) isolated from edible mushroom has a potent anti-proliferative effect on malignant colon cells with considerable therapeutic potential as an anti-neoplastic agent. Since previous studies on the structural requirement for binding were limited to molecular or submolecular levels of Galβ1-3GalNAc (T; Thomsen–Friedenreich disaccharide glycotope; where Gal represents d-galactopyranose and GalNAc represents 2-acetamido-2-deoxy-d-galactopyranose) and its derivatives, the binding properties of ABA were further investigated using our collection of glycans by enzyme-linked lectinosorbent assay and lectin–glycan inhibition assay. The results indicate that polyvalent Galβ1-related glycotopes, GalNAcα1-Ser/Thr (Tn), and their cryptoforms, are the most potent factor for ABA binding. They were up to 5.5×105 and 4.7×106 times more active than monomeric T and GalNAc respectively. The affinity of ABA for ligands can be ranked as: multivalent Tα (Galβ1-3GalNAcα1-), Tn and I/II (Galβ1-3GlcNac/Galβ1-4GlcNAc, where GlcNAc represents 2-acetamido-2-deoxy-d-glucopyranose)>>>>monomeric Tα and Tn>I>>GalNAc>>>II, L (Galβ1-4Glc, where Glc represents d-glucopyranose) and Gal (inactive). These specific binding features of ABA establish the importance of affinity enhancement by high-density polyvalent (versus multiantennary I/II) glycotopes and facilitate our understanding of the lectin receptor recognition events relevant to its biological activities.

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