Archive 23/8/24

Aberrant glycosylation in serum glycoproteins observed in patients with Hashimoto’s thyroiditis

A group from Department of Laboratory Medicine, Shengjing Hospital of China Medical University, Shenyang, China, etc. has reported about aberrant glycosylation observed in Hashimoto’s thyroiditis.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10348014/

Hashimoto’s thyroiditis (HT) is the most common autoimmune thyroid disorder and is characterized by lymphocyte infiltration of the parenchyma and the presence of antibodies specific to thyroid antigens.
In this study, a total of 53 serum samples collected from 27 patients with HT and 26 healthy controls (HCs) were used for lectin microarray analysis, and it was found that the majority of the lectin binding signals in HT group were weakened compared with the HC group, while the Vicia villosa agglutinin (VVA) binding signal was increased.


Mx thinks that the quality of lectin microarrays used was not GOOD enough.

KLF12/Gal-1 axis may serve as a novel cancer therapeutic target for patients with immunotherapy resistance

A group from Department of Thoracic Surgery, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China, etc. has reported that KLF12/Gal-1 axis may serve as a novel cancer therapeutic target for patients with immunotherapy resistance.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10432659/

In this study, it was demonstrated that the decline in KLF12 in tumor cells is an important mechanism for immune escape, leading to resistance to anti-PD-1 therapy. Mechanistically, KLF12 could directly bind to the promoter region of Gal-1 and inhibit its expression, and thereby promotes CD8+ T cell infiltration into the tumor microenvironment and kills tumore cells.

Continued research into the mechanisms of action of KLF12 and a new combination immunotherapy for circumventing drug resistance may provide more effective treatment options for patients with cancer.

A lectibody comprised of a dimeric fragment of the Shiga toxin B-subunit (StxB) and the human CD3 antibody fragment

A group from Faculty of Biology, University of Freiburg, 79104 Freiburg, Germany, etc. has reported about a bispecific lectibody boosting T cell cytotoxicity towards Gb3-positive cancer cells.
https://www.mdpi.com/2073-4409/12/14/1896

A lectibody, comprised of a dimeric fragment of the Shiga toxin B-subunit (StxB) and the human CD3 antibody(clone No. UCHT1)fragment, was produced in E. coli and purified via Ni-NTA affinity chromatography. The StxB-scFv UCHT1 lectibody has bispecificity to T-cells and Gb3-positive cancer cells. The Shiga toxin B-subunit (StxB) can selectively target Gb3-positive cancer cells, and cytotoxic T cells are activated via UCFT1.

In this paper, it was shown that the lectibody could induce the killing of up to 80% of Gb3-overexpressing cancer cells in haemorrhagic and solid tumours.

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