Last year, the Structural Antibody Database (SAbDab) listed a record-breaking 894 new antibody structures, driven in no small part by the continued efforts of the researchers to understand SARS-CoV-2.
In this blog post I wanted to highlight the major driving force behind this curve – the huge increase in cryo electron microscopy (cryoEM) data – and the implications of this for the field of structure-based antibody informatics.
Today’s group meeting was the GOAT (Greatest Of ALL Time) as we were honoured with the presence of Daisy (professional internet goat) from Cronkshaw Farm.
My first post of the year is about another major change to the way the World Health Organisation will be assigning “International Non-proprietary Name”s (INNs) to antibody-based therapeutics. I haven’t seen this publicised widely, so I thought I’d share it here as it is an important consideration for anyone mining or exploiting this data.
I recently spoke at the Festival of Biologics 2021 conference in Basel (in-person, just in time!), and was lucky enough to be offered the chance to chair a session of talks. As this was the first time I’d ever been asked to do this, I asked Charlotte for some hints to make things go more smoothly. I found her advice very useful, so I thought I’d share it here for other first-time “chairers”!
Earlier this month the World Health Organisation (WHO) released Proposed International Nonproprietary Name List 125 (PL125), comprising the therapeutics entering clinical trials during the first half of 2021. We have just added this data to our Therapeutic Structural Antibody Database (Thera-SAbDab), bringing the total number of therapeutic antibodies recognised by the WHO to 711.
Back in May 2020, we released the Coronavirus Antibody Database (‘CoV-AbDab’) to capture molecular information on existing coronavirus-binding antibodies, and to track what we anticipated would be a boon of data on antibodies able to bind SARS-CoV-2. At the time, we had found around 300 relevant antibody sequences and a handful of solved crystal structures, most of which were characterised shortly after the SARS-CoV epidemic of 2003. We had no idea just how many SARS-CoV-2 binding antibody sequences would come to be released into the public domain…
10 months later (2nd March 2021), we now have tracked 2,673 coronavirus-binding antibodies, ~95% with full Fv sequence information and ~5% with solved structures. These datapoints originate from 100s of independent studies reported in either the academic literature or patent filings.
Last Wednesday, I was fortunate enough to be invited as a guest lecturer to the 3rd BioDataScience101 workshop, an initiative spearheaded by Paolo Marcatili, Professor of Bioinformatics at the Technical University of Denmark (DTU). This session, on amino acid sequence analysis applied to both proteomics and antibody drug discovery, was designed and organised by OPIG’s very own Tobias Olsen.
The start of Michaelmas Term means some new faces on our Zoom screens and lots of things for our new group members to get used to. To help them settle in quickly I thought I’d put together an updated edition of the 10 Commandments of OPIG, tailored towards our new reality.
Since my last blogpost on this topic back in 2018, OPIG has expanded its range of tools for antibody/BCR analysis. Here is an updated summary of the OPIG antibody databases and immunoinformatics tools.
I came across a recent paper on the antibody-protein binding and conformational changes. As I work mainly on the binding site/Fv regions of antibodies, I am intrigued to see the role of the constant domains in the overall antibody function.