jin rongsheng uc irvine brands

Structure and function of bacterial toxins and receptors; synaptic proteins; protein complexes; protein-protein and protein-ligand interactions; X-ray crystallography; high-throughput screening

Our research group is dedicated to understand the molecular basis of human diseases using structural biology, which allows us to visualize how proteins function or malfunction at the atomic level. Our current research is focused on three areas: (1) exploring the molecular mechanisms underlying the toxic and therapeutic functions of botulinum neurotoxins (BoNTs), which will help to develop effective anti-BoNT strategies and improve clinical applications of BoNT; (2) characterizing the structures of Clostridium difficile (C. diff) toxins (TcdA and TcdB) and their interactions with host receptors, and understanding how they contribute to the disease of Clostridium difficile infection (CDI) that tops the CDC’s list of urgent threats; (3) advancing mechanistic understanding of ion channels, receptors, and signaling molecules in the nervous system, which will facilitate the design and improvement of therapeutic agents for the treatment of some psychological and neurological disorders. We are also developing cutting-edge small molecule high-throughput screening (HTS) assays based on our understanding of the structure and function of these disease-related proteins, which may lead to novel chemical probes and/or drug candidates for basic research and therapeutic application.

Lam, K. H., Guo, Z., Krez, N., Matsui, T., Perry, K., Weisemann, J., Rummel, A., Bowen, M. E. & Jin, R. A viral-fusion-peptide-like molecular switch drives membrane insertion of botulinum neurotoxin A1. Nat Commun 9, 5367 (2018) doi: 10.1038/s41467-018-07789-4.

Chen, P., Tao, L., Liu, Z., Dong, M. & Jin, R. Structural insight into Wnt signaling inhibition by Clostridium difficile toxin B. FEBS J (2018) doi: 10.1111/febs.14681.

Chen, P., Tao, L., Wang, T., Zhang, J., He, A., Lam, K. H., Liu, Z., He, X., Perry, K., Dong, M*. & Jin, R*. Structural basis for recognition of frizzled proteins by Clostridium difficile toxin B. Science 360, 664-669 (2018) (*corresponding authors) doi: 10.1126/science.aar1999. PMCID: PMC6231499

Lam, K. H., Sikorra, S., Weisemann, J., Maatsch, H., Perry, K., Rummel, A., Binz, T. & Jin, R. Structural and biochemical characterization of the protease domain of the mosaic botulinum neurotoxin type HA. Pathog Dis 76 (2018) doi: 10.1093/femspd/fty044. PMCID: PMC5961070

Silva, D. A., Stewart, L., Lam, K. H., Jin, R. & Baker, D. Structures and disulfide cross-linking of de novo designed therapeutic mini-proteins. FEBS J 285, 1783-1785 (2018) doi: 10.1111/febs.14394. PMCID: PMC6001749

Lam, K. H., Qi, R., Liu, S., Kroh, A., Yao, G., Perry, K., Rummel, A. & Jin, R. The hypothetical protein P47 of Clostridium botulinum E1 strain Beluga has a structural topology similar to bactericidal/permeability-increasing protein. Toxicon 147, 19-26 (2018) doi: 10.1016/j.toxicon.2017.10.012. PMCID: PMC5902665

Chevalier, A., Silva, D.A., Rocklin, G.J., Hicks, D.R., Vergara, R., Murapa, P., Bernard, S.M., Zhang, L., Lam, K.H., Yao, G., Bahl, C.D., Miyashita, S.I., Goreshnik, I., Fuller, J.T., Koday, M.T., Jenkins, C.M., Colvin, T., Carter, L., Bohn, A., Bryan, C.M., Fernández-Velasco, D.A., Stewart, L., Dong, M., Huang, X., Jin, R., Wilson, I.A., Fuller, D.H. & Baker, D. Massively parallel de novo protein design for targeted therapeutics. Nature 550(7674):74-79 (2017) doi: 10.1038/nature23912. PMCID: PMC5802399

Yao, G., Lam, K.H., Weisemann, J., Peng, L., Krez, N., Perry, K., Shoemaker, C.B., Dong, M., Rummel, A. & Jin, R. A camelid single-domain antibody neutralizes botulinum neurotoxin A by blocking host receptor binding. Sci Rep. 7;7(1):7438. (2017) doi: 10.1038/s41598-017-07457-5. PMCID: PMC5547058

Yao, G., Lam, K.H., Perry, K., Weisemann, J., Rummel, A. & Jin, R. Crystal Structure of the Receptor-Binding Domain of Botulinum Neurotoxin Type HA, Also Known as Type FA or H. Toxins (Basel) 9, 93 (2017) doi: 10.3390/toxins9030093. PMCID: PMC5371848

Yao, G., Zhang, S., Mahrhold, S., Lam, K. H., Stern, D., Bagramyan, K., Perry, K., Kalkum, M., Rummel, A.*, Dong, M.* & Jin, R.* N-linked glycosylation of SV2 is required for binding and uptake of botulinum neurotoxin A. Nat Struct Mol Biol 23 (7):656-662 (2016) (*corresponding authors) doi: 10.1038/nsmb.3245. PMCID: PMC5033645

Lee, K., Lam, K. H., Kruel, A. M., Mahrhold, S., Perry, K., Cheng, L. W., Rummel, A. & Jin, R. Inhibiting oral intoxication of botulinum neurotoxin A complex by carbohydrate receptor mimics. Toxicon 107, 43-49 (2015) doi: 10.1016/j.toxicon.2015.08.003. PMCID: PMC4658216

Lam, K.H. & Jin, R. Architecture of the botulinum neurotoxin complex: a molecular machine for protection and delivery. Current Opinion in Structural Biology 31:89-95 (2015) doi: 10.1016/j.sbi.2015.03.013. PMCID: PMC4476938

Lam, K.H., Yao, G. & Jin, R. Diverse binding modes, same goal: The receptor recognition mechanism of botulinum neurotoxin. Progress in Biophysics and Molecular Biology 117(2-3):225-31 (2015) doi: 10.1016/j.pbiomolbio.2015.02.004. PMCID: PMC4417461

Lam, T.I., Stanker, L.H., Lee, K., Jin, R. & Cheng, L.W. Translocation of botulinum neurotoxin serotype A and associated proteins across the intestinal epithelia. Cellular Microbiology 17(8):1133-1143 (2015) doi: 10.1111/cmi.12424. PMCID: PMC4610714

Matsui, T.*, Gu, S., Lam, K.H., Carter, L.G., Rummel, A., Mathews, II. & Jin, R.* Structural Basis of the pH-Dependent Assembly of a Botulinum Neurotoxin Complex. J. Mol. Biol. 426(22):3773-3782 (2014) doi: 10.1016/j.jmb.2014.09.009. (*corresponding authors) PMCID: PMC4252799

Lee, K., Zhong, X., Gu, S., Kruel, A.M., Dorner, M.B., Perry, K., Rummel, A., Dong, M. & Jin, R. Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex. Science 344(6190):1405-1410 (2014) doi: 10.1126/science.1253823. PMCID: PMC4164303

Lee, K., Lam, K.H., Kruel, A.M., Perry, K., Rummel, A. and Jin, R. High-resolution crystal structure of HA33 of botulinum neurotoxin type B progenitor toxin complex. Biochem. Biophys. Res. Commun. 446(2):568-573 (2014) doi: 10.1016/j.bbrc.2014.03.008. PMCID: PMC4020412

Yao, Y., Lee, K., Gu, S., Lam, K.H. & Jin, R. Botulinum Neurotoxin A Complex Recognizes Host Carbohydrates through Its Hemagglutinin Component, Toxins (Basel) 6(2):624-635 (2014) doi: 10.3390/toxins6020624. PMCID: PMC3942755

Lee, K., Gu, S., Jin, L., Le, T.T.N., Cheng, L.W., Strotmeier, J., Kruel, A.M., Yao, G., Perry, K., Rummel, A.* & Jin, R.* Structure of a Bimodular Botulinum Neurotoxin Complex Provides Insights into Its Oral Toxicity. PLoS Pathog. 9(10): e1003690 (2013) doi:10.1371/journal.ppat.1003690. (*corresponding authors) PMCID: PMC3795040

Zong, Y. and Jin, R. Structural mechanisms of the agrin-LRP4-MuSK signaling pathway in neuromuscular junction differentiation. Cell. Mol. Life Sci. 70(17):3077-88 (2013) doi: 10.1007/s00018-012-1209-9. PMCID: PMC4627850

Gu, S. and Jin, R. Assembly and function of the botulinum neurotoxin progenitor complex. Curr. Top. Microbiol. Immunol. 364:21-44 (2013) doi: 10.1007/978-3-642-33570-9_2. PMCID: PMC3875173

Gu, S., Rumpel, S., Zhou, J., Strotmeier, J., Bigalke, H., Perry, K., Shoemaker, C.B., Rummel, A. & Jin, R. Botulinum neurotoxin is shielded by NTNHA in an interlocked complex. Science 335(6071):977-81 (2012) doi: 10.1126/science.1214270. PMCID: PMC3545708

Zong, Y., Zhang, B., Gu, S., Lee, K., Zhou, J., Yao, G., Figueiredo, D., Perry, K., Mei, L.* & Jin, R.* Structural basis of neuron-specific regulation of postsynaptic differentiation. Gene & Development 26:247-258 (2012) doi: 10.1101/gad.180885.111. (*corresponding authors) PMCID: PMC3278892

Yao, G., Zong, Y., Gu, S., Zhou, J., Xu, H., Mathews, II. & Jin, R. Crystal structure of the glutamate receptor GluA1 amino-terminal domain. Biochem. J. 438(2):255-63 (2011) doi: 10.1042/BJ20110801. PMCID: PMC3296483

Strotmeier, J., Gu, S., Jutzi, S., Mahrhold, S., Zhou, J., Pich, A., Eichner, T., Bigalke, H., Rummel, A.*, Jin, R.* & Binz, T*. The biological activity of botulinum neurotoxin type C is dependent upon novel types of ganglioside binding sites. Mol. Microbiol. 81(1):143-56 (2011) doi: 10.1111/j.1365-2958.2011.07682.x. Epub 2011 Jun 2. (*corresponding authors)

Strotmeier, J., Lee, K., Völker, A.K., Mahrhold, S., Zong, Y., Zeiser, J., Zhou, J., Pich, A., Bigalke, H., Binz, T., Rummel, A.* & Jin, R.* Botulinum neurotoxin serotype D attacks neurons via two carbohydrate-binding sites in a ganglioside-dependent manner. Biochem. J. 431(2):207-16 (2010) (*corresponding authors)

Jin, R.*, Singh, S.K., Gu, S., Furukawa, H., Sobolevsky, A.I., Zhou, J., Jin, Y. & Gouaux E.* Crystal structure and association behavior of the GluR2 amino-terminal domain. EMBO J. 28(12):1812-23 (2009) (*corresponding authors) PMCID: PMC2699365

Kumar, J., Schuck. P., Jin, R. & Mayer, M.L. The N-terminal domain of GluR6-subtype glutamate receptor ion channels. Nat. Struct. Mol. Biol. 16(6):631-8 (2009) PMCID: PMC2729365

Jin, R., Rummel, A., Binz, T. & Brunger, A.T. Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity. Nature 444:1092-5 (2006)

Jin, R., Clark, S., Weeks, A.M., Dudman, J.T., Gouaux, E. & Partin, K.M. Mechanism of positive allosteric modulators acting on AMPA receptors. J. Neurosci. 25(39):9027-36 (2005)

Jin, R., Junutula, J.R., Matern, H.T., Ervin, K.E., Scheller, R.H. & Brunger, A.T. Exo84 and Sec5 are competitive regulatory Sec6/8 effectors to the RalA GTPase. EMBO J. 24:2064-74 (2005)

Jin, R., Bank, T., Mayer, M. L., Traynelis, S. & Gouaux, E. Structural basis for partial agonist action at ionotropic glutamate receptors. Nat. Neurosci. 6(8):803-10 (2003)

Structure of the glucosyltransferase domain of TcdA in complex with RhoA provides insights into substrate recognition. Sci Rep. 2022 05 30; 12(1):9028.

Jahid S, Ortega JA, Vuong LM, Acquistapace IM, Hachey SJ, Flesher JL, La Serra MA, Brindani N, La Sala G, Manigrasso J, Arencibia JM, Bertozzi SM, Summa M, Bertorelli R, Armirotti A, Jin R, Liu Z, Chen CF, Edwards R, Hughes CCW, De Vivo M, Ganesan AK. PMID: 35385746; PMCID: PMC9127750.

Probing the structure and function of the protease domain of botulinum neurotoxins using single-domain antibodies. PLoS Pathog. 2022 01; 18(1):e1010169.

Chen P, Zeng J, Liu Z, Thaker H, Wang S, Tian S, Zhang J, Tao L, Gutierrez CB, Xing L, Gerhard R, Huang L, Dong M, Jin R. PMID: 34145250; PMCID: PMC8213806.

Structural Insights into Rational Design of Single-Domain Antibody-Based Antitoxins against Botulinum Neurotoxins. Cell Rep. 2020 02 25; 30(8):2526-2539.e6.

Chen P, Lam KH, Liu Z, Mindlin FA, Chen B, Gutierrez CB, Huang L, Zhang Y, Hamza T, Feng H, Matsui T, Bowen ME, Perry K, Jin R. PMID: 31308519; PMCID: PMC6684407.

The hypothetical protein P47 of Clostridium botulinum E1 strain Beluga has a structural topology similar to bactericidal/permeability-increasing protein. Toxicon. 2018 Jun 01; 147:19-26.

High-resolution crystal structure of HA33 of botulinum neurotoxin type B progenitor toxin complex. Biochem Biophys Res Commun. 2014 Apr 04; 446(2):568-73.

Botulinum neurotoxins are produced by Clostridium botulinum and cause the possibly fatal disease botulism, which impedes nerve cells ability to communicate with muscles and can lead to paralysis and respiratory failure. The botulinum toxin has also been identified as a potential biological weapon against a civilian population.

Currently, there is no efficient countermeasure for this toxin in case of a large outbreak of botulism, Jin said. Our discovery provides a vital first step toward a pharmaceutical intervention at an early point that can limit the toxins fatal attack on the human body.

Jin added that his work opens the door to further development of preventive treatments for botulism. At the same time, the molecular gateway for the lethal toxin could be exploited for alternative applications, such as the oral delivery of protein-based therapeutics.

Kwangkook Lee, Shenyan Gu and Guorui Yao of UC Irvine; Lei Jinof the Sanford-Burnham Medical Research Institute in La Jolla, Calif.; Thi Tuc Nghi Le, Jasmin Strotmeier and Anna Magdalena Kruelof the Institute for Toxicology at Germanys Hannover Medical School; Luisa W. Cheng of the U.S. Department of Agriculture; and Kay Perry of Cornell University contributed to the study, which was supported in part by the National Institute of Allergy & Infectious Diseases (grants R01AI091823 and U54 AI065359), the German Research Foundation, the Swiss Federal Office for Civil Protection and the U.S. Department of Agriculture CRIS project (grant 5325-42000-048-00D).

Led by UCI professor of molecular biology & biochemistry Christopher C.W. Hughes, the research team successfully established multiple vascularized micro-organs on an industry-standard 96-well plate. Hughes and the study’s first author, Duc T. T. Phan, showed that these miniature tissues are much better at reproducing human drug responses than previous model systems. Hughes and his…

Botulinum toxin (Botox) is a large protein that is composed of three domains (upper right corner, crystal structure shown in yellow, green, and pink). The new study reveals a novel mechanism by which the toxin hijacks three receptors on the host neuronal surface as its “GPS” — the peptide moiety of protein SV2 (green-blue ribbon model), a conserved glycan modification of SV2 (green and light blue sticks), and a lipid (brown sticks) — to launch its attack. Source: Rongsheng Jin and Guorui Yao / UCI

A study co-led by Rongsheng Jin, professor of physiology & biophysics at the University of California, Irvine; Min Dong with Boston Children’s Hospital-Harvard Medical School; and Andreas Rummel with the Hannover Medical School in Germany, reveals an important general mechanism by which the pathogen is attracted to, adapts to and takes advantage of glycan modifications in surface receptors to invade motor neurons. Glycans are chains of sugars synthesized by cells for their development, growth, functioning or survival. Results appear June 13 in Nature Structural and Molecular Biology.

“Our findings reveal a new paradigm of the everlasting host-pathogen arms race, where a pathogen develops a smart strategy to achieve highly specific binding to a host receptor while also tolerating genetic changes on the receptor,” Jin said. “And to some extent, this mechanism by which the toxin attacks human is similar to the one that is utilized by some important broad-neutralizing human antibodies to fight viruses, such as dengue viruses and HIV.”

Botulinum neurotoxin A (BoNT/A), commonly known as the Botox toxin, is widely used in a weakened form for treating various medical conditions as well as for cosmetics. The clinical product Botox contains extremely low doses of the toxin and is safe to use. But at higher doses, it can be lethal, and it’s also classified as a potential bioterrorism agent.

The intricate detail of how the Botox toxin recognizes its receptors also reveals novel ways to neutralizing these deadly toxins. “With this new structural information,” Rummel said, “we were able to pinpoint key amino acids in the toxin that are required for binding to sugars, and we found that even mutating a single amino acid is sufficient to abolish the toxicity by more than a million fold.”

Guorui Yao and Kwok-ho Lam at UCI, Sicai Zhang at Harvard, Stefan Mahrhold at the Hannover Medical School, Daniel Stern at Berlin’s Center for Biological Threats & Special Pathogens, Kay Perry at the Argonne National Laboratory in Illinois, and Karine Bagramyan and Markus Kalkum the Beckman Research Institute at the City of Hope in Duarte, Calif., contributed to the study, which was primarily supported by the National Institutes of Health.

SimRated is a UC Irvine (UCI) startup that provides online simulation training programs for medical procedures with a mission to improve patient safety by effectively training healthcare workers and students to perform these procedures through simulation-based training. Co-founder and CEO Dr. Cameron Ricks, clinical professor of Anesthesiology and director of the Medical Education Simulation Center at UCI’s School of Medicine, and his team have honed the program’s development and are now in revenue, reaching hundreds of students in their path to startup success.

For over a decade, Ricks has taught anesthesiology and, during his time as the director of the Medical Education Simulation Center, began to realize a potential venture in online simulation training.

“Cameron and I work toward standardizing medical education, particularly in medical simulation for increased competence and patient safety down the line,” said Beaulieu. “We have customers in high school career and technical education programs using our products to learn how to do vital signs and suturing, all the way to the other side of the continuum with advanced airway techniques for medical students.”

“We’re having fun with it; it’s an entrepreneurial adventure. It’s education for us; we’re learning, we get to interact with high school students and teachers,” said Ricks. “We also get to interact with the clinical experts who help develop the videos.”

“Education is changing and people are looking to see what’s out there and are interested in online options, especially in spaces where they may not have that primary education because having a physician or nurse come into the classroom is not always possible because these clinicians are busy,” said Ricks. “We solve that problem by coming into the classroom remotely and I think that’s part of what attracts the teachers, as well.”

Though the world’s switch to online learning has been beneficial for the startup’s impact on high school educational reach, SimRated experienced their first sale about a year and half ago. Currently, their primary clientele, high school teachers, range in location from the Bay Area to Los Angeles Unified School District and local school districts in Orange County.

Since its launch, the SimRated team has utilized UCI Beall Applied Innovation’s resources and programs to help the startup progress. Because Ricks was using his own capital to initially fund the company, Ricks consulted with licensing officers to ensure he was launching the startup through the appropriate UCI avenues. The team also took part in the I-Corps program, Applied Innovation’s market discovery program funded by the National Science Foundation, and have since joined the Wayfinder incubator, where the team remains as they move their startup forward.

“Our first customer came to because Juan Felipe [Vallejo] introduced me to an Innovation Advisor who said I should call this high school,” said Ricks. “So, I called and that was our first customer.”

Looking ahead, the team plans to study the growth of their startup, during and post-pandemic as well as expand into more high schools. SimRated also wants to move into higher education, like junior colleges and medical schools, Ricks says, each one with their own separate market and learning curves.

“My hope is one day this grows big enough that I can work for fun and stay at UCI because I enjoy it,” said Ricks. “I think I have many years until that happens, so I’m not quitting my day job anytime soon.”

Researchers from the University of California, Irvine and Harvard University have discovered how the Clostridium difficile toxin B (TcdB) recognizes the human Frizzled protein, the receptor it uses to invade intestinal cells and lead to deadly gastrointestinal infections. The findings could pave the way for new C. diff antitoxins and also show potential for the development of novel anti-cancer drugs.

In a C. diff infection (CDI), TcdB targets colonic epithelia and binds to what are called Frizzled (FZD) receptors. Researchers in the labs of Rongsheng Jin, PhD , professor of physiology & biophysics from the UCI School of Medicine, and Min Dong, PhD , from Boston Children"s Hospital - Harvard Medical School, found that during this binding process, the toxin locks certain lipid molecules in FZD, which block critical Wnt signaling that regulates renewal of colonic stem cells and differentiation of the colonic epithelium.

"This toxin is indeed very smart. It takes advantage of an important lipid that FZD uses for its own function, to improve its binding affinity and specificity to FZD," said Jin, "However, the need for this lipid also exposes a vulnerability of TcdB that could be exploited to develop antitoxins that block toxin-receptor recognition."

Jin and Dong believe that the novel FZD-antagonizing mechanism exploited by toxin B could be used to turn this deadly toxin into a potential pharmacological tool for research and therapeutic applications, including anti-cancer drugs.

New research has revealed the first 3D structure of the Clostridioides difficile toxin B (TcdB) in complex with chondroitin sulfate proteoglycan 4 (CSPG4), a human receptor. According to researchers from the University of California, Irvine School of Medicine, this could help future efforts to develop new therapeutics for the prevention and treatment of C. difficile.

“TcdB is one of two homologous C. difficile exotoxins, which are major virulence factors responsible for the spread of C. difficile infections,” said senior author Rongsheng Jin, PhD, a professor in the University of California–Irvine department of Physiology and Biophysics, in the press release. “TcdB alone is capable of causing the full spectrum of diseases associated with [Clostridioides difficile infection] in humans.

“What these new findings tell us is that a rationally designed CSPG4-mimicking decoy could neutralize major TcdB vairants, providing a unique therapeutic avenue for combating some of the hyper-virulent C. difficile strains,” Jin said in the press release.

In contrast, the investigators found that the therapeutic mechanism for bezlotoxumab, the only FDA-approved anti-TcdB antibody, is sensitive to escaping mutations in some bacterial strains. The current standard of care for C. difficile infections includes treatments that use broad spectrum antibiotics, which frequently lead to recurrence. Although bezlotoxumab could reduce the recurrence rate among some patients, results from this and earlier studies suggest that it has weaker potency against some variants.

“We have designed a CSPG4-mimicking decoy based on the 3D structure we observed,which could neutralize major TcdB variants and is superior to bezlotoxumab on a major TcdB variant from a hyper-virulent strain (TcdB2) in our studies,” Jin explained in the press release. “As a highly conserved cellular receptor of TcdB, a CSPG4 decoy molecule would be difficult for TcdB to escape, since any mutations that disrupt toxin binding to the decoy would also disrupt binding to its native receptors.”

“We are now examining the therapeutic features of these novel antitoxin molecules, and we believe they could provide broad-spectrum protection and neutralization against most known TcdB variants, thus improving existing antibody therapeutics for [Clostridioides difficile infection],” Jin concluded.

Study reveals new therapeutic target for C. difficile infection. News release. University of California, Irvine School of Medicine. June 18, 2021. Accessed June 22, 2021. https://som.uci.edu/news_releases/Therapeutic-target-for-C-difficile-infection.asp

Gavin Herbert, founder of Irvine-based drug maker Allergan Inc., is keeping mum on his creation’s effort to fight off a hostile takeover bid by Valeant Pharmaceuticals International Inc.

“Another ophthalmologist helped us with an idea of a product called Blephamide, which became our No. 1 product when we moved to Orange County. In ’61, we had our first real lab production facility, 30,000 square feet in Santa Ana.

He called Allergan’s first 10 years of existence “so instructive because you kind of had to do everything yourself. You wore a lot of hats—you got out and spent time with your customers, [for example].”

Herbert also emphasized the importance of hiring the right executives. He said that Allergan hired roughly eight veterans from companies, such as Merck & Co. and SmithKline (now part of GlaxoSmithKline PLC), when it moved from Los Angeles to Orange County.

Herbert is “truly the founder and chairman of Orange County’s position as the leader in ophthalmic innovation,” according to Matthew Jenusaitis, Octane’s chief executive, who introduced Herbert and Mazzo’s interview.

Researchers at the University of California-Irvine School of Medicine said they’ve found out how bacterial toxins that cause food-borne botulism are absorbed through the intestinal lining and into the bloodstream.

UC Irvine associate professor of physiology and biophysics Rongsheng Jin and colleagues found that a series of botulinum neurotoxin compounds bind with patients’ epithelial cell proteins. That initiates a process that disrupts intercellular seals

“By identifying this … process by which the toxin compound manages to open the door from inside, we can better understand how to seek new methods to prevent these deadly toxins from entering the bloodstream,” Jin said in a news release.

Researchers from Harvard University, Hannover Medical School’s Institute for Toxicology in Germany, the Center for Biological Threats and Special Pathogens in Berlin, and the Argonne National Laboratory joined Jin and other UCI faculty in working on the project.

PersonalCare, a concierge medical practice that also manages Hoag Memorial Hospital Presbyterian’s executive health program, said it moved its corporate headquarters to a new office in Irvine. The practice has also doubled its number of affiliated doctors from five to 10 over the past 18 months. … Aliso Viejo-based UST Global said it would enter the patient-centered health information technology market. It’s working with Silver Spring, Md.-based Amida Technology Solutions to develop healthcare software and other products.

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David M. Aronoff, Vanderbilt University Medical Center, USA Martha R.J. Clokie, University of Leicester, UK Craig Ellermeier, University of Iowa, USA Yukako Fujinaga. Kanazawa University, JPN Lindsay Hall, Quadram Institute of Bioscience, UK Rongsheng Jin, University of California, Irvine, USA Ed J. Kuijper, Leiden University Medical Center, NL Trevor Lawley, Wellcome Trust Sanger Institute, UK Mauricio Navarro, University of California, Davis, USA Ornella Rossetto, University of Pavia, ITA Olga Soutourina, Université Paris-Sud, FRA Sarah Tschudin-Sutter, University Hospital Basel, SUI Mark Wilcox, Leeds Teaching Hospitals, NHS Trust, UK Vincent B. Young, University of Michigan, USA Joseph P. Zackular, University of Pennsylvania, USA