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Dec 1, 2015 | Blogs, Life Science Research, Proteomics | 0 comments
SWATH® Acquisition: On the Forefront of HIV-1 Research
World AIDS Day is held on the 1st December each year and is an opportunity for people worldwide to unite in the fight against HIV, show their support for people living with HIV, and to commemorate people who have died. World AIDS Day was the first ever global health day, held for the first time in 1988.
Source: http://www.worldaidsday.org/about
A research team at the University of Nebraska Medical Center (UNMC) is using SWATH Acquisition to advance a host-oriented antiviral strategy that targets the biomolecules required for viral replication.
Using SWATH for quantitative proteomics together with bioinformatic analyses to identify host proteins, the team quantified the expression of 3,608 proteins in uninfected and HIV-1-infected monocyte-derived microphages.
Of these, they found that 420 were significantly altered upon HIV-1 infection, and the findings highlighted a novel set of proteins and processes that are involved in the host response to HIV-1 infection.
Journal of Proteomics Research, 2014, April 4; Drs. P. Ciborowski, N. Haverland, H. Fox, University of Nebraska Medical Center or VIEW the webinar (May 2014) by Drs. Pawel Ciborowski and Nicole Haverland
In this informative presentation, you’ll learn:
Finding the right information shouldn’t slow you down. Whether you’re troubleshooting your mass spec, learning something new, or optimizing performance, access to the right resources at the right moment makes all the difference.
As an analytical strategy, middle-down mass spectrometry (MS) workflows characterize biotherapeutic proteins by analyzing large, digested protein fragments or defined subunits, rather than fully intact proteins (top-down) or digested peptides (bottom-up). A middle-down strategy combines the strengths of top-down and bottom-up approaches by delivering high sequence coverage and structural specificity while maintaining relatively simple sample preparation. In practice, middle-down analysis enables accurate mass measurement, rapid sequence confirmation, and localization of key post-translational modifications (PTMs) on protein subunits that are directly relevant to product quality.
In biopharmaceutical development, sequence variants (SV) are considered an inherent risk of producing complex proteins in living systems. Sequence variants are unintended changes to the amino acid sequence of a biotherapeutic and can be caused by errors in transcription or translation in the host cell, or cell culture and process conditions. Detailed analysis of SVs is important in process and product development to ensure the drug’s safety and efficacy. Even low‑level sequence variants can have significant implications for product quality, safety, and efficacy, making their accurate detection and characterization a critical requirement across development, process optimization, and regulatory submission.
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