Researchers at La Jolla Institute for Immunology, Scripps Research, and the Ragon Institute of MGH, MIT, and Harvard report coordinated studies showing that several HIV germline-targeting immunogens can be delivered together to activate multiple broadly neutralizing antibody precursors.

HIV vaccine design faces the challenge that B cells capable of maturing into broadly neutralizing antibodies (bnAb) are exceptionally rare and poorly stimulated by standard antigens. Most immune responses concentrate on variable parts of the viral envelope rather than the conserved regions that would enable cross-strain protection from HIV.

Germline-targeting immunogens have been developed to engage those rare naive B cells directly, but until now, each construct was tested in isolation, leaving open whether several could be given at once without interference. In paired studies published in Science Immunology, investigators tested that question across two models using different vaccine formats.

Mitochondria, the primary energy-producing organelles in eukaryotic cells, power essential biosynthetic processes through oxidative phosphorylation [1]. These organelles are highly dynamic and continually undergo cycles of fusion and fission to support energy-demanding cellular activities such as proton pumping for gastric acid secretion [2]. These membrane remodeling events are regulated by evolutionarily conserved guanosine triphosphatases (GTPases) from the dynamin superfamily, with fusion at the outer and inner membranes mediated by MFN1/2 and OPA1, respectively, and fission occurring by Drp1 [3]. However, little is known about how Drp1 anchors to the mitochondrial outer membrane. Here, we report a previously uncharacterized protein, C3orf33, as a novel adaptor for Drp1 and designate it Mitofissin (MiSN) on the basis of its function in controlling mitochondrial fission. Our preliminary screen suggested that MiSN localizes to mitochondria. To visualize dynamic and fine MiSN localization, we transiently transfected U2OS cells to express green fluorescent protein (GFP)-MiSN, followed by real-time imaging using lattice structured illumination microscopy (Lattice SIM). As shown in Figure 1 A, MiSN colocalized with the mitochondrial dye MitoTracker. Careful examination of the zoomed-in image revealed that the MiSN signal was exterior to the MitoTracker (Figure 1 A, arrow). Further characterization of the cellular fractions revealed that MiSN was enriched in the mitochondrial fraction (Figure 1 B). Thus, we concluded that MiSN is a novel mitochondrial outer membrane protein.

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Scientists from the A*STAR Infectious Diseases Labs (A*STAR IDL) have uncovered a surprising mechanism showing how mosquito saliva can alter the human body’s immune response during chikungunya virus (CHIKV) infection, contributing to Singapore’s broader efforts to strengthen infectious disease preparedness.

The research, published in Nature Communications, reveals that sialokinin, a bioactive peptide in Aedes mosquito saliva, binds to neurokinin receptors on immune cells and suppresses monocyte activation, thereby reducing inflammation and facilitating early viral dissemination. These findings offer new insight into how mosquito bites shape disease outcomes.

Background: acute mesenteric ischemia (AMI) is a life-threatening condition that is caused by inadequate blood flow through the mesenteric vessel and is related to high mortality rates due to systemic complications. This study aims to systematically review the available literature concerning the major findings of possible biomarkers for early detection of acute mesenteric ischemia in the human population. Methods: studies that measured the performance of biomarkers during acute mesenteric ischemia were identified with the search of PubMed, Embase, Medline, and Cochrane library. Results: from a total of 654 articles, 46 articles examining 14 different biomarkers were filtered, falling within our inclusion criteria. Intestinal fatty acid-binding protein (I-FABP) was the most commonly researched biomarker regarding AMI, with sensitivity ranging from 61.5% to 100% and specificity ranging from 40% to 100%. The second most commonly researched biomarker was D-dimer, with a sensitivity of 60–100% and a specificity of 18–85.71%. L-lactate had a sensitivity of 36.6–90.91% and a specificity of 64.29–96%. Several parameters within the blood count were examined as potential markers for AMI, including NLR, PLR, MPV, RDW, DNI, and IG. Citrulline, interleukin 6 (IL-6), and procalcitonin (PCT) were the least-researched biomarkers. Conclusion: different biomarkers showed different accuracies in detecting AMI. I-FABP and D-dimer have been the most researched and shown to be valuable in the diagnosis of AMI, whereas L-lactate could be used as an additional tool. Ischemia-modified albumin (IMA), alpha glutathione S-transferase (αGST), interleukin 6 (IL-6), and citrulline showed potential use in their respective studies. However, further research needs to be done on larger sample sizes and with controls to reduce bias. Several studies showed that neutrophil–lymphocyte ratio (NLR), platelet–lymphocyte ratio (PLR), mean platelet volume (MPV), red-cell distribution width (RDW), delta neutrophil index (DNI), and immature granulocytes (IGs) might be useful, as well at the same time be widely distributed and affordable in combination with other markers presenting higher specificity and sensitivity.

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