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Related Concept Videos

Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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Translation01:31

Translation

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Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of...
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Translation01:31

Translation

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Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
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Proteins are...
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Histone Modification02:32

Histone Modification

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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
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Initiation of Translation02:33

Initiation of Translation

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Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
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Termination of Translation01:44

Termination of Translation

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The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
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Author Spotlight: Quantitative Detection of DNA Protein Crosslinks and Their Post-Translational Modifications
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Author Spotlight: Quantitative Detection of DNA Protein Crosslinks and Their Post-Translational Modifications

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Harnessing post-translational modifications for next-generation HIV immunogens.

Joel D Allen1, Rogier W Sanders2,3, Katie J Doores4

  • 1Centre for Biological Sciences and Institute for Life Sciences, University of Southampton, Southampton SO17 1BJ, U.K.

Biochemical Society Transactions
|May 23, 2018
PubMed
Summary

Designing vaccines against the human immunodeficiency virus (HIV) is challenging due to complex envelope spike modifications. However, targeting these unique glycan shields with engineered antigens offers a promising strategy for developing broadly neutralizing antibodies (bnAbs).

Keywords:
glycobiologyglycosylationimmunogenvaccinevirus

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Area of Science:

  • Virology
  • Immunology
  • Vaccine Design

Background:

  • The human immunodeficiency virus (HIV) envelope spike is heavily modified with over 30 disulfide bonds and approximately 100 N-linked glycosylation sites.
  • These modifications create a dense glycan shield that obscures conserved epitopes, posing a significant challenge for vaccine development.
  • Protease cleavage within the secretory system is essential for the functional maturation of the envelope spike.

Purpose of the Study:

  • To explore the challenges and opportunities presented by HIV envelope spike post-translational modifications for vaccine design.
  • To investigate the potential of targeting the glycan shield with broadly neutralizing antibodies (bnAbs).
  • To assess the utility of engineered envelope spike mimetics in guiding bnAb development through vaccination.

Main Methods:

  • Analysis of the structural and functional characteristics of HIV envelope spike glycoproteins.
  • Investigation of the role of N-linked glycosylation and disulfide bonds in viral structure and immune evasion.
  • Development and evaluation of recombinant envelope spike mimetics with re-engineered post-translational modifications.

Main Results:

  • The mature HIV envelope spike adopts a compact fold, with its surface largely covered by a glycan shield.
  • Despite glycosylation heterogeneity, specific B-cell lineages can recognize and neutralize diverse viral strains.
  • Engineered envelope spike mimetics aim to present stable antigens that can elicit broadly neutralizing antibodies.

Conclusions:

  • The complex post-translational modifications of the HIV envelope spike present both challenges and opportunities for vaccine development.
  • Targeting the glycan shield with bnAbs is a promising avenue for HIV vaccine design.
  • Advanced recombinant envelope spike mimetics hold potential for guiding the development of effective bnAb-inducing vaccines.