KIAA0319L

Last update 08 May 2025

Basic Info

Synonyms

AAVR, Adeno-associated virus receptor, Dyslexia-associated protein KIAA0319-like protein

+ [3]

Introduction

Possible role in axon guidance through interaction with RTN4R. (Microbial infection) Acts as a receptor for adeno-associated virus and is involved in adeno-associated virus infection through endocytosis system.

100 Clinical Results associated with KIAA0319L

100 Translational Medicine associated with KIAA0319L

0 Patents (Medical) associated with KIAA0319L

Literatures (Medical) associated with KIAA0319L

01 Mar 2025·Molecular Therapy Methods & Clinical Development

A versatile cell line for establishing potency of cell type-specific AAV transgenes

Article

Author: Lein, Ed S ; Mich, John K ; Groce, Erin L ; Levi, Boaz P ; Martinez, Refugio A ; Bishaw, Yemeserach M ; Gore, Bryan B ; Quinlan, Meagan A

Potency assays are essential for adeno-associated virus (AAV) therapy development, allowing simple and quantitative assessments of therapeutic activity, target engagement, vector stability, and activity per batch. However, cell culture-based AAV potency assays are generally hampered by two limitations: (1) commonly used cell lines have low AAV transduction efficiency due to their lack of appropriate surface receptors, and (2) cell type-specific AAV transgenes are often not expressed because their regulatory elements (enhancers, promoters, etc.) may not be active in the cell lines used for testing. Here, we present the CRISPR activation-AAV receptor (CRAAVR) cell line, a stable HEK293T-derived line that overcomes both problems. CRAAVR cells constitutively express the AAV receptor (AAVR) and an AAV-targeted CRISPR transactivator, and, as a result, exhibit high transduction efficiency and drive transgene expression from AAVs with cell type-specific regulatory elements. Furthermore, CRAAVR cells can assess AAV transgene potency in a quantitative manner, as demonstrated by gamma-aminobutyric acid (GABA) uptake of an AAV-delivered GABA transporter (GAT-3). Due to their greater transduction efficiency, regulatory element-agnostic expression, and utility as a potency assay tool, CRAAVR cells will help streamline the development and validation of AAV-based reagents and therapeutics.

08 Jan 2025·mBio

Identification of SLC35A1 as an essential host factor for the transduction of multi-serotype recombinant adeno-associated virus (AAV) vectors

Article

Author: McFarlin, Shane ; Qiu, Jianming ; Zhang, Xiujuan ; Ning, Kang ; Richart, Donovan ; Feng, Zehua ; Zhang-Chen, Ander ; Yan, Ziying ; McFarlane, Richenda ; Cheng, Fang ; Hao, Siyuan ; Aksu Kuz, Cagla

ABSTRACT We conducted a genome-wide CRISPR/Cas9 screen in suspension 293 F cells transduced with rAAV5. The highly selected genes revealed after two rounds of screening included the previously reported KIAA0319L , TM9SF2 , and RNF121 , along with a cluster of genes involved in glycan biogenesis, Golgi apparatus localization, and endoplasmic reticulum penetration. In this report, we focused on solute carrier family 35 member A1 ( SLC35A1 ), a Golgi apparatus-localized cytidine 5’-monophosphate-sialic acid (CMP-SIA) transporter. We confirmed that SLC35A1 knockout (KO) significantly decreased rAAV5 transduction to a level lower than that observed in KIAA0319L or TM9SF2 KO cells. Although SLC35A1 KO drastically reduced the expression of α2,6-linked SIA on the cell surface, the expression of α2,3-linked SIA, as well as the cell binding and internalization of rAAV5, was only moderately affected. Moreover, SLC35A1 KO significantly diminished the transduction of AAV multi-serotypes, including rAAV2 and rAAV3, which do not utilize SIAs for primary attachment. Notably, the SLC35A1 KO markedly increased transduction of rAAV9 and rAAV11, which primarily attach to cells via binding to galactose. Further analyses revealed that SLC35A1 KO significantly decreased vector nuclear import. More importantly, although the C-terminal cytoplasmic tail deletion (∆C Tail) mutant of SLC35A1 did not drastically decrease SIA expression, it significantly decreased rAAV transduction, as well as vector nuclear import, suggesting that the C-tail is critical in these processes. Furthermore, the T128A mutant significantly decreased SIA expression but still supported rAAV transduction and nuclear import. These findings highlight the involvement of the CMP-SIA transporter in the intracellular trafficking of rAAV vectors post-internalization. IMPORTANCErAAV is an essential tool for gene delivery in the treatment of genetic disorders; however, the mechanisms of rAAV transduction remain partially understood. GPR108 is vital for the transduction of most rAAV vectors, but not for rAAV5. We aimed to identify host factors that impact AAV5 transduction akin to GPR108. Using a genome-wide CRISPR/Cas9 screen in 293 F cells, we identified SLC35A1, a Golgi apparatus-localized CMP-sialic acid transporter that transports CMP-sialic acid from the cytoplasm into the Golgi apparatus for sialylation, is essential to rAAV transduction. Further studies across various AAV serotypes showed SLC35A1 significantly affects vector nuclear import post-internalization. These results underscore the crucial role of SLC35A1 in intracellular trafficking beyond the initial cell attachment of rAAV.

17 Oct 2024·The Journal of Physical Chemistry B

Coarse-Grained Simulations of Adeno-Associated Virus and Its Receptor Reveal Influences on Membrane Lipid Organization and Curvature

Article

Author: Pipatpadungsin, Nichakorn ; Rouse, Sarah L. ; Chao, Kin

Adeno-associated virus (AAV) is a well-known gene delivery tool with a wide range of applications, including as a vector for gene therapies. However, the molecular mechanism of its cell entry remains unknown. Here, we performed coarse-grained molecular dynamics simulations of the AAV serotype 2 (AAV2) capsid and the universal AAV receptor (AAVR) in a model plasma membrane environment. Our simulations show that binding of the AAV2 capsid to the membrane induces membrane curvature, along with the recruitment and clustering of GM3 lipids around the AAV2 capsid. We also found that the AAVR binds to the AAV2 capsid at the VR-I loops using its PKD2 and PKD3 domains, whose binding poses differs from previous structural studies. These first molecular-level insights into AAV2 membrane interactions suggest a complex process during the initial phase of AAV2 capsid internalization.

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KIAA0319L

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