Robin G Bombardi

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Researchers studied how the human immune system reacts to a pig kidney transplant in a brain-dead human. They found that specific immune cells in the blood increased significantly, leading to rejection of the kidney by day 33 after the transplant. This research is important because it helps identify ways to improve the success of pig organ transplants in humans, potentially addressing the shortage of available human organs for transplantation.

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Researchers transplanted a pig kidney-thymus combination into a deceased human and tracked the immune response over 61 days. T cells from the recipient infiltrated the organ and specific clones expanded in blood, tissue, and lymph nodes around rejection events. This reveals that T cell-driven rejection of pig organs in humans closely mirrors what happens with human-to-human transplants, informing how future immunosuppression strategies must be designed.

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This study examined how many stroke patients in Italy's Veneto region actually received clot-dissolving drugs or mechanical clot removal between 2017 and 2021, and whether access was equal across the region's different zones. Treatment rates exceeded European targets overall, but the proportion of patients receiving thrombectomy varied significantly depending on which area they lived in. The results show that geography still determines who gets the most advanced stroke care and call for reorganizing how hospitals are networked to fix this inequality.

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Scientists isolated antibodies from the blood of yellow fever vaccine recipients, screened them for their ability to block viral infection, and identified one antibody, YFV-136, that potently neutralized multiple wild-type yellow fever strains. YFV-136 was then tested in hamsters and in mice carrying human liver cells, and it protected against lethal yellow fever challenge in both models. This antibody is a strong candidate therapeutic for yellow fever, a disease that currently has no approved antiviral treatment.

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Researchers used computational protein-modeling software to scan large databases of antibody sequences from hepatitis C-infected patients and find antibodies that share an unusual structural feature — a disulfide bond within a key binding loop — associated with broad virus neutralization. They identified new members of this antibody family and analyzed what amino acid patterns determine their shape. Understanding these structural rules can guide the design of vaccines that reliably trigger this particularly effective type of antibody response.

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Researchers used five different DNA sequencing technologies to comprehensively map structural changes in the genome of a breast cancer reference cell line — the large-scale rearrangements like deletions, duplications, and translocations that point mutations alone don't capture. By combining all methods and verifying the results with independent techniques, they assembled a high-confidence catalog of 1,788 structural variants in the cancer genome. This reference set gives researchers a reliable benchmark for evaluating and improving tools used to detect cancer-related genomic rearrangements.

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Researchers analyzed outcomes from 512 stroke patients treated across 25 hospitals in northeast Italy in 2018 to determine whether faster treatment times actually translated into better recovery and whether outcomes differed between large stroke centers and smaller ones. Three-month outcomes were similar regardless of hospital level, but faster time to thrombectomy — the mechanical removal of clots — was strongly and consistently linked to better functional outcomes. The study makes a concrete case for reorganizing the regional stroke network to reduce the time it takes to transfer patients from smaller hospitals to centers that perform thrombectomy.

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This study looked at what happened to stroke care in northeast Italy — a region of roughly 7 million people — during the first wave of COVID-19 in early 2020, comparing the number of patients admitted to stroke units and treated before versus during the lockdown. Stroke admissions and thrombectomy procedures dropped significantly during lockdown, while clot-dissolving drug treatment rates held steady. The findings show that emergency clot-removal surgery was disproportionately disrupted during the pandemic, raising concerns about how stroke networks function under crisis conditions.

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Researchers isolated antibodies from people who were naturally infected with Rift Valley fever virus or vaccinated with an experimental vaccine and identified antibodies that potently neutralize the virus by blocking it from fusing with cells. In mouse experiments, representative antibodies from multiple binding sites reduced illness and death when given before or after infection. This study identifies multiple antibody candidates for human use and reveals that blocking the virus fusion mechanism — not just attachment — is a key route to strong neutralization of this emerging pathogen.

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This study identified a group of human antibodies from multiple different people that all target the same newly discovered weak point on the influenza A virus — the interface between the three identical subunits of the hemagglutinin protein — and found that these antibodies share common genetic and structural features despite coming from unrelated individuals. The shared features suggest this is a "public" antibody response that the immune system reliably generates. Because this epitope is highly conserved across influenza A strains, it is a promising target for a universal flu vaccine.

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Researchers used a combination of single-cell gene sequencing and mass spectrometry-based proteomics to identify which Ebola-specific antibodies from memory B cells actually circulate in the blood plasma of a survivor, finding that only a fraction of the large pool of Ebola-specific B cell antibodies contributed to circulating plasma antibodies. The antibodies detected in plasma predominantly targeted two sites on the Ebola glycoprotein — the glycan cap and the base region — and many were capable of neutralizing the virus. These results show that a small subset of antibody specificities does most of the protective work in recovered Ebola patients, which has direct implications for vaccine design.

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Researchers studied immune responses in two people who had recovered from H7N9 avian influenza — a bird flu virus that can infect humans and could trigger a pandemic — mapping which parts of the virus surface protein their antibodies recognized. The antibodies targeted a diverse range of sites on the protein and used varied mechanisms to block the virus, including preventing it from entering cells and disrupting the protein's structure. The breadth and functional diversity of this natural immune response provides a detailed guide for designing vaccines against avian H7N9 influenza.

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Researchers isolated human antibodies from a person previously vaccinated against Hendra virus and found two classes that worked together synergistically — one blocking the virus from attaching to cells and one that was actually enhanced by receptor binding — to neutralize the related Nipah virus. In a hamster model of lethal Nipah infection, combining antibodies from both classes was more protective than either class alone. This synergy suggests these antibodies are good candidates for a cocktail therapeutic against Hendra and Nipah viruses, which have no approved treatments.

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A two-antibody cocktail was developed that can protect against all three major forms of Ebola virus that infect humans — Ebola, Sudan, and Bundibugyo viruses — by targeting two non-overlapping sites on the virus surface glycoprotein. In non-human primate studies, the cocktail was highly effective as therapy even after infection had begun. This is the first broadly protective antibody treatment to demonstrate efficacy against all three medically relevant ebolaviruses, addressing a critical gap because existing approved drugs only work against Ebola virus.

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Researchers determined the structural and molecular basis for why a human antibody, ZIKV-116, neutralizes Zika virus but also cross-reacts with certain dengue virus strains. The antibody blocks viral entry after the virus attaches to cells by targeting a specific region on the viral envelope, and a single amino acid difference between Zika strains, and between Zika and dengue, explained the differences in how well the antibody worked. These findings clarify the molecular details of cross-reactive immunity between Zika and dengue and have implications for vaccine design.

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Researchers analyzed the antibody repertoires of Ebola survivors to find two antibodies that bind to non-overlapping sites on the Ebola glycoprotein and work cooperatively — one helping the other bind more effectively by remodeling the glycan sugar coating on the viral surface. High-resolution structures revealed how molecular mimicry shapes how these antibodies engage the virus. In non-human primates, the two-antibody cocktail protected against Ebola disease and the virus could not easily escape by mutating, showing that cooperative antibody pairs can solve both the potency and resistance problems of single antibody treatments.

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Researchers isolated human antibodies from people with prior Ross River fever — an arthritis-causing mosquito-borne virus widespread in Australia — and identified antibodies that strongly block infection through multiple mechanisms, including preventing the virus from attaching to the recently identified Mxra8 receptor. In mouse studies, these antibodies prevented disease and reduced viral levels in multiple tissues. The work maps the major targets on the Ross River virus surface recognized by human immunity and identifies therapeutic antibody candidates.

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This study tested how well a blood test for MOG-IgG antibodies — markers associated with a distinct type of inflammatory brain disease — identifies the right patients when applied to adults who had a first episode of nerve inflammation that didn't clearly fit multiple sclerosis. Using a revised set of clinical criteria beyond the official 2018 recommendations, the sensitivity of the test increased from 28 to 42 percent while specificity remained high. The results suggest that adjusting which patients are tested for MOG antibodies could substantially improve the diagnostic yield in clinical practice.

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Scientists isolated human antibodies against enterovirus D68 (EV-D68), a virus that causes respiratory illness and increasingly is linked to acute flaccid myelitis — a polio-like paralysis in children — and identified one antibody, EV68-228, that broadly neutralized diverse strains and protected mice from both respiratory disease and neurological damage. Cryo-electron microscopy revealed how two potent antibodies attach to different positions on the virus particle, suggesting distinct blocking mechanisms. These findings indicate that antibodies are a key part of protection against EV-D68 neurological disease and identify clinical candidates.

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Researchers used next-generation sequencing of antibody genes from bone marrow samples to identify the dominant light chain clone in patients with AL amyloidosis — a disease where a misfolded antibody fragment accumulates in organs and causes damage. The method successfully detected the disease-causing clone and also revealed that the overall antibody repertoire is disrupted in different patterns across different patients. This proof-of-concept study suggests that antibody gene sequencing could be developed into a clinical tool for detecting residual disease in amyloidosis patients.

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Researchers sequenced the complete T cell receptor repertoires of multiple healthy individuals and found that a surprisingly large fraction — around 8 to 11 percent of T cell receptor sequences — are shared between unrelated people. The shared fraction was higher in naive T cells than memory T cells, suggesting these common sequences arise from the genetics of recombination rather than shared infections. Cataloging these shared T cell receptor sequences provides a resource for studying how T cells respond to diseases and could reveal common immune response signatures.

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Researchers developed a way to deliver a potently neutralizing Zika antibody as an mRNA molecule — rather than as a purified protein — packaged in a lipid nanoparticle designed for injection into muscle rather than intravenous infusion. In mice, this intramuscular mRNA delivery protected against lethal Zika virus challenge both before and after infection. Making antibody therapy injectable into muscle rather than requiring an IV infusion would make it far more practical to deploy during outbreaks in resource-limited settings.

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Researchers developed and demonstrated a rapid end-to-end pipeline — combining single-cell RNA sequencing, bioinformatics, and mRNA delivery technology — that can go from isolating antibodies from human donors to testing them in animals within 78 days during a simulated outbreak response. Applying this to Zika virus, they screened over 100 antibodies, identified 29 broadly neutralizing candidates, and validated the best ones in mice and non-human primates using both protein and mRNA delivery approaches. This pipeline provides a blueprint for accelerating antibody drug development in response to emerging viral threats.

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Researchers identified human antibodies that broadly neutralize a group of viruses — arthritogenic alphaviruses including chikungunya, Ross River, and Mayaro — all by targeting the same conserved site on the virus surface where the virus binds the recently discovered Mxra8 receptor. Cryo-electron microscopy structures showed the same antibody footprint across three different alphaviruses, and the lead antibody protected mice from disease. Because this epitope is conserved, it is an attractive target for a single vaccine or drug that could work against multiple related alphaviruses.

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Researchers developed a computational method that uses the three-dimensional structure of a single known antibody to score large sequence databases and find other antibodies that likely fold into the same binding shape, even if their sequences look different. Applying this method to the flu-specific antibody CH65, they identified new antibodies with similar structures and antiviral activity, confirmed by crystal structures and virus inhibition tests. This approach enables mining of immune repertoire data to find antibodies with desired properties without requiring structural experiments on every candidate.

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Researchers developed antibodies targeting NS1 — a Zika virus protein not found on the virus particle itself — and showed that these antibodies can protect both pregnant and non-pregnant mice from Zika infection without causing the antibody-dependent enhancement effect that makes anti-envelope antibodies potentially dangerous. Protection depended on the antibodies binding tightly to NS1 on the surface of infected cells and activating immune killing mechanisms. This demonstrates that NS1-targeted antibodies are a viable alternative strategy for preventing congenital Zika disease.

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Researchers isolated ultrapotent human antibodies from a survivor of eastern equine encephalitis virus (EEEV), one of the deadliest viruses in North America, and used cryo-electron microscopy to determine exactly how two of them bind and block the virus. Both antibodies protected mice from lethal EEEV infection delivered as an aerosol, which is the exposure route of concern if the virus were used as a bioweapon. The structural information identifies the molecular targets that effective EEEV vaccines and drugs need to engage.

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Researchers isolated the first known human antibodies against Hendra virus from a patient with prior exposure, identified five distinct sites on the viral attachment protein that these antibodies can target, and found that two of the most potent cross-reactive antibodies protected ferrets from lethal Nipah virus infection up to three days after exposure. Crystal structures of the two lead antibodies revealed exactly how they block the virus. These antibodies are promising prophylactic drug candidates and the epitopes they target define sites for rational vaccine design against Hendra and Nipah viruses.

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Researchers identified and characterized the first fully human monoclonal antibodies against IsdA, a surface protein that Staphylococcus aureus uses to transfer iron-containing heme during infection. Two antibodies reduced bacterial burden in a mouse model of blood infection through complementary mechanisms — directly blocking heme transfer and activating immune cell killing via the antibody's Fc region. These results show that targeting multiple aspects of the bacterial iron theft system with antibodies is a viable antibacterial strategy.

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Researchers isolated antibodies from four US Ebola survivors within 1 to 3 months of hospital discharge and found that early after recovery, Ebola-specific memory B cells were rare and most produced antibodies that could not neutralize the virus. One neutralizing antibody, EBOV237, was identified and shown to protect mice from lethal Ebola infection at levels comparable to an approved antibody drug. The results reveal that the human antibody response is slow to mature after Ebola infection and highlight the glycan cap as an important target for early vaccine responses.

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Researchers sequenced the B cell antibody repertoires of several individuals and found that — contrary to prior assumption — a large fraction of antibody sequences are shared between unrelated people: up to 6% of heavy chains and up to 34% of light chains between any two individuals. Many of these shared sequences were found even in cord blood, indicating that some common antibody structures arise from genetics of the recombination process rather than from shared infections. Knowing which antibody sequences are commonly generated across humans has implications for understanding immune responses and designing broadly effective vaccines.

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Researchers solved crystal structures of an Ebola-survivor antibody, BDBV223, bound to a conserved region of the Ebola glycoprotein stalk and found that it neutralizes two different ebolaviruses by locking the three arms of the glycoprotein in an open position, disrupting the structure needed for viral membrane fusion. Targeted mutations to the antibody aimed at extending its activity to a third ebolavirus (Sudan) suggested that additional binding contacts outside the visualized region are needed. These structural insights inform engineering of antibodies with broader ebolavirus coverage.

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Researchers discovered a naturally occurring human antibody, FluA-20, that binds to a previously unknown site on influenza A hemagglutinin — the interface between the three identical subunits of the protein — and neutralizes nearly all influenza A strains by destabilizing this interface and blocking cell-to-cell spread of the virus. The antibody protected mice against four different influenza A subtypes. This discovery identifies a highly conserved site of vulnerability on influenza hemagglutinin that could be targeted by next-generation universal flu vaccines and treatments.

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Researchers isolated ultrapotent human antibodies against chikungunya virus from an infection survivor, encoded the best one as an mRNA molecule packaged in lipid nanoparticles, and showed that a single injection into muscle protected mice from arthritis, tissue infection, and death from chikungunya. In monkeys, this mRNA delivery achieved antibody blood levels well above the threshold needed for protection in mice, with sustained levels after a second dose. The results establish mRNA-encoded antibodies as a practical approach for protecting against chikungunya, a globally spreading virus with no approved treatments.

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Researchers found that a specific antibody gene segment (IGHV3-30) commonly produces human antibodies that target IsdB, a protein Staphylococcus aureus uses to steal iron from human hemoglobin during infection, and showed these antibodies work through at least three distinct mechanisms including directly blocking iron acquisition and activating immune killing. Structural studies revealed how antibodies from this gene segment engage multiple different sites on IsdB. These findings advance understanding of natural immunity to staph infections and point to therapeutic strategies targeting the bacterial iron acquisition system.

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Researchers isolated 35 human antibodies against the neuraminidase (NA) surface protein of H7N9 avian influenza from survivors and vaccinees, finding that all of them worked by preventing newly made virus particles from being released from infected cells — a different mechanism than most influenza antibodies. The antibodies recognized multiple different sites on NA, yet all used this same blocking mechanism to protect mice from lethal infection in both preventive and treatment settings. The results suggest that vaccines stimulating NA-specific antibodies could complement existing hemagglutinin-focused influenza vaccines.

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Researchers developed a method called repertoire fingerprinting that reduces the complexity of large antibody gene sequence datasets to just two dimensions using principal component analysis, making it possible to identify patterns shared between people with the same disease or immune exposure. Applied to data from people with different diseases and vaccination histories, the method successfully grouped individuals with common immune experiences. This computational approach could eventually be developed into a diagnostic tool based on patterns in a person's antibody repertoire.

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Researchers sequenced the antibody repertoires of multiple HIV-infected individuals from before infection through chronic disease and identified "public" antibody sequences that appeared in multiple unrelated donors during HIV infection. Some of these shared sequences were also found at low levels in people never exposed to HIV, suggesting a common precursor is regularly generated by the immune system. Identifying these public clonotypes points to specific antibody blueprints that HIV vaccines could aim to reliably trigger.

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Researchers identified a human antibody, H3v-47, that broadly neutralizes both human H3N2 influenza and the emerging swine-origin H3N2 variant strains that caused severe human cases, and determined it binds a unique site on hemagglutinin that spans two subdomains not previously targeted by any known neutralizing antibody. The antibody works mainly by trapping virus inside infected cells and also kills infected cells through immune system recruitment. This newly defined conserved site is a target for designing vaccines that protect against both human and swine H3 influenza strains.

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Researchers identified a broadly neutralizing human antibody, EBOV-520, from Ebola survivors that targets the base of the Ebola glycoprotein — a site shared across Ebola, Sudan, and Bundibugyo viruses — and showed it works through multiple mechanisms including direct neutralization and immune cell activation. EBOV-520 protected animals from all three ebolaviruses in relevant disease models. This antibody is a strong candidate for development as a pan-ebolavirus therapeutic and defines a conserved target on the glycoprotein base that vaccines should aim to engage.

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Researchers isolated 25 human antibodies against the GII.4 Sydney 2012 strain of norovirus — the dominant strain behind hundreds of outbreaks since 2012 — and identified antibodies that block the virus from attaching to cell receptors and can neutralize live virus in human gut tissue grown from stem cells. The antibodies targeted three main sites on the viral surface, defining the landscape of neutralizing immunity. This work establishes the first well-characterized human neutralizing antibodies against norovirus, which kills around 200,000 people per year and has no approved vaccine.

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Researchers measured whether fat-like Gb3 deposits in skin biopsies distinguish patients with Fabry disease who have classical disease-causing gene mutations from those with milder late-onset variants, using a fluorescence method in 52 genetically defined patients. Gb3 deposits were found in all classical mutation patients but not in those with late-onset variants or in disease controls, and patients with deposits had less nerve fiber in the skin than those without. Skin Gb3 deposits are a specific marker for classical Fabry disease and appear to cause nerve damage indirectly rather than by accumulating inside nerve fibers.

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This multicenter study characterized the clinical features and antibody subtypes in patients testing positive for MOG antibodies — markers of a distinct inflammatory brain and spinal cord disease separate from MS — and found that optic nerve and spinal cord involvement were most common, relapses occurred in half of patients, and IgG1 was the dominant antibody subclass though others were present. Testing showed that MOG antibody levels tended to decrease in patients who didn't relapse. The study confirms that MOG antibody-associated disease has a recognizable clinical profile and that subclass analysis may add diagnostic and prognostic information.

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This study measured blood levels of neurofilament light chain — a protein released when nerve cells are damaged — in patients with inflammatory spinal cord and optic nerve diseases, comparing those with AQP4 antibodies versus MOG antibodies versus neither. Patients with AQP4 antibodies had significantly higher neurofilament levels than those with MOG antibodies or no antibodies, indicating more severe ongoing nerve damage. This suggests that the type of antibody a patient has predicts the extent of nerve injury and potentially the aggressiveness of their disease.

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Researchers isolated a panel of human antibodies from Zika survivors and identified one, ZIKV-117, that neutralized both African and Asian-American strains of Zika by targeting a unique site at the junction between adjacent envelope protein dimers on the virus surface. In pregnant mice, treatment with ZIKV-117 dramatically reduced Zika infection in the placenta and fetus, tissue damage, and death. This antibody demonstrates that human antibodies can prevent mother-to-fetus transmission of Zika and defines a structural target for Zika vaccine design.