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Secret to how cholera adapts to temperature revealed

The Cava group and their international collaborators at the European Molecular Biology Laboratory (EMBL), Harvard Medical School and Ohio State University have discovered an essential protein in cholera-causing bacteria that allows them to adapt to changes in temperature, according to a study published today in eLife.

Text by Emily Packer, Media Relations Manager, eLife

Impact statement: A protein that helps Vibrio cholerae adapt to temperature has been identified, providing insights into how bacteria change their biology under different conditions.

The protein, BipA, is conserved across bacterial species, which suggests it could hold the key to how other types of bacteria change their biology and growth to survive at suboptimal temperatures.
Vibrio cholerae (V. cholerae) is the bacteria responsible for the severe diarrhoeal disease cholera. As with other species, V. cholerae forms biofilms – communities of bacteria enclosed in a structure made up of sugars and proteins – to protect against predators and stress conditions. V. cholerae forms these biofilms both in their aquatic environment and in the human intestine. There is evidence to suggest that biofilm formation is crucial to V. cholerae’s ability to colonise in the intestine and might enhance its infectivity.

“V. cholerae experiences a wide range of temperatures, and adapting to them is not only important for survival in the environment but also for the infection process,” explains lead author Teresa del Peso Santos, a postdoctoral researcher at the Laboratory for Molecular Infection Medicine Sweden (MIMS), Umeå University, Sweden. “We know that at 37 degrees Celsius, V. cholerae grows as rough colonies that form a biofilm. However, at lower temperatures these colonies are completely smooth. We wanted to understand how it does this.”

Today, we celebrate women and girls in science

It is the 11th of February, marking the International Day of Women and Girls in Science.

This day allows us to direct more attention to the still ongoing inequalities between genders in academia, andcontinue working together towards a day when gender biases and discrimination are defeated worldwide. On a global level, women in STEM positions (Science, Technology, Engineering, Math) are still rare and according to the UN, only 30% of researchers are women. They publish less, get paid less and their careersalso progress slower and often not as far as for men. Scientists at MIMS were asked to fill out a survey, anonymously, on what it means for them to be a female scientist, and more than half of the participants answered that “I am a scientist, no matter which gender.”While others thought:

“It means I appreciate all female scientists that have broken down the barriers before me and given me a seat at the table. I am also aware of the work we still have to do, the mentoring of young female scientists to ensure that e.g., faculty positions become much more gender balanced.”

“I never thought that gender played a role in being good at a certain career, but I learned that subconsciously kids can be conditioned to think that jobs are for a certain gender just because if you google 'scientist' mostly photos of men come up. If me being a female scientist can encourage a child to be one, then that's amazing.”

Annual Call for PhD Students by the Nordic EMBL Partnership

The Nordic EMBL Partnership for Molecular Medicine has opened its annual call for recruting outstanding PhD students. The Partnership consists of four nodes, residing at the universities of Oslo in Norway, Umeå in Sweden, Helsinki in Finnland and Aarhus in Denmark. These excellent research centres offer a fantastic PhD education and research experience with state-of-the-art technologies and strong networking. To find out more, read more at https://projects.au.dk/nordic-embl-partnership/show-news/artikel/nordic-embl-partnership-annual-call-for-phd-students/ (written by Annabel Darby, Joint Communications Officer Nordic EMBL Partnership & NCMM) and follow the indicated instructions for all details, or open the PDF file.

Nordic_EMBL_PhD_call_2021.pdf

Solving the structure of diarrhea virus by two virologists in Umeå

Niklas Arnberg and Lars-Anders Carlson (researchers at Umeå University and MIMS, Umeå) recently published the atomic level structure of the enteric human adenovirus 41 using cryo-electron microscopy. This type of virus is responsible for diarrhea and related complications in children. To find out more, please go to: https://www.umu.se/en/news/breakthrough-on-diarrhea-virus-opens-up-for-new-vaccines_9989218/ (article written by Ola Nilsson, communication officer at Umeå University). The original scientific publication is available at: https://advances.sciencemag.org/content/7/2/eabe0974 .