Enrichment Program

Establishing A Binding Assay To Probe The Interaction Between Trim5alpha And The Hiv-1 Capsid Protein

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Human immunodeficiency virus 1 (HIV-1) has persistently been a global health concern, infecting 39
million people around the world with 1.3 million cases increment in 2020, leading to severe
immunodeficiency (UNAIDS, 2023). While mammalian genomes show evidence of repeated infection
with retroviral pathogens, this co-evolution has resulted in the emergence of defense mechanisms
that prevent and contain infection, such as Trim5α. These proteins guard against cross-species
transmission, yet their precise mechanisms still require to be found (Saha et al., 2020). The known
information is that Trim5α acts during early stages of the retroviral life cycle, preventing reverse
transcription and integration. To do this Trim5α must recognise and interact with the retroviral capsid
(Keown et al., 2016). While much is known about this interaction, the molecular details of binding are
poorly understood. Hence, to investigate the binding, the SPRY domain was expressed through the
yeast display method, and examined its interaction with HIV-1 capsids through fluorescence
microscopy. However, the binding between SPRY domain and HIV-1 capsid was not detected. This
could be caused by several factors, including that the expression of the SPRY domain was not fully
expressed on the surface of the yeast. More deeper research on the expression of SPRY domain should
be done for better understanding and done a binding with HIV-1 capsid.

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Detail Information

Series Title

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Call Number

EP BM-031

Publisher

i3L, Jakarta : i3L, Jakarta., 2024

Collation

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Language

English

ISBN/ISSN

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Classification

EP BM-031

Content Type

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Media Type

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Carrier Type

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Edition

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Subject(s)

HIV-1
Trim5a
SPRY domain
Yeast display
Fluorescence microscopy

Specific Detail Info

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Statement of Responsibility

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