AAV1-hSyn-FLuc

The exact origin of the first serotype of AAV (AAV1) remains unknown, as it was not originally isolated from tissue but rather as a contaminant of an adenoviral vector, and antibodies to it have been found in both humans and non-human primates (NHPs). This serotype uses sialic acid as its primary cell surface receptor and the AAV receptor (AAVR) as a coreceptor. According to Rabinowitz J.E. et al., AAV1 does not bind to heparin because it lacks the amino acid residues R585 and R588 required for such binding and therefore cannot be purified using heparin. Zolotukhin S. et al. developed a protocol for the chromatographic purification of AAV1 by iodixanol gradient centrifugation and anion exchange chromatography. It can also be purified using a mucin column, as it can bind to sialic acid residues in mucin. In addition, a systematic analysis of ten AAV serotypes by Mary B. et al. showed that recombinant AAV1 (rAAV1) showed no detectable post-translational modifications (PTMs), and it was the first viral vector approved for gene therapy.

In 1999, Xiao W. et al. conducted a study to explore viral vectors for gene therapy and found that AAV1 was the most effective serotype for skeletal muscle transduction. Since then, many studies have confirmed that AAV1 has a higher tropism for skeletal muscle from mice, dogs, and non-human primates compared to other serotypes. AAV1 has also been found to be able to effectively transduce neurons, glial cells, and ependymal cells in the mouse brain. In addition, it has been found to be able to effectively transduce the heart, endothelial cells, vascular smooth muscle, and retina.