Tetraspanins - Gateways for Infection

Monk, Peter N.; Partridge, Lynda J.

doi:10.2174/187152612798994957

Cited by 69 publications

(60 citation statements)

References 209 publications

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“…Tetraspanins participate in the infection by several viruses, bacteria or protozoa (Monk and Partridge, 2012). Many studies have unravelled a role of tetraspanins in the entry of the pathogen.…”

Section: Box 1 Tetraspanins In Infectious Diseasesmentioning

confidence: 99%

“…Several tetraspanins are recruited to the budding site of HIV (Krementsov et al, 2010) and are incorporated into the viral membrane (Monk and Partridge, 2012). Furthermore, the presence of tetraspanins at exit sites and in viral particles inhibits, to some extent, virus infection at a post-attachment step, as well as the formation of syncytium induced by the virus (Gordón-Alonso et al, 2006;Krementsov et al, 2009;Sato et al, 2008).…”

Section: Box 1 Tetraspanins In Infectious Diseasesmentioning

confidence: 99%

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Tetraspanins at a glance

Charrin

Jouannet

Boucheix

et al. 2014

Journal of Cell Science

377

371

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Tetraspanins are a family of proteins with four transmembrane domains that play a role in many aspects of cell biology and physiology; they are also used by several pathogens for infection and regulate cancer progression. Many tetraspanins associate specifically and directly with a limited number of proteins, and also with other tetraspanins, thereby generating a hierarchical network of interactions. Through these interactions, tetraspanins are believed to have a role in cell and membrane compartmentalization. In this Cell Science at a Glance article and the accompanying poster, we describe the basic principles underlying tetraspaninbased assemblies and highlight examples of how tetraspanins regulate the trafficking and function of their partner proteins that are required for the normal development and function of several organs, including, in humans, the eye, the kidney and the immune system.

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Section: Box 1 Tetraspanins In Infectious Diseasesmentioning

confidence: 99%

Section: Box 1 Tetraspanins In Infectious Diseasesmentioning

confidence: 99%

Tetraspanins at a glance

Charrin

Jouannet

Boucheix

et al. 2014

Journal of Cell Science

377

371

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“…Importantly, CD151 forms stoichiometric complexes with laminin-binding integrins (e.g., ␣3␤1 and ␣6␤1/4), and most of its known functions are intricately linked to these integrins (40,41). TERM are used by various viruses, such as hepatitis C virus (HCV), HIV-1, and influenza virus as molecular platforms for their entry and postentry stages during infection (42)(43)(44)(45). One of the first discoveries was the identification of tetraspanin CD81 as a ligand for HCV.…”

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confidence: 99%

Tetraspanin CD151 Mediates Papillomavirus Type 16 Endocytosis

Scheffer

Gawlitza

Spoden

et al. 2013

J Virol

118

171

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cHuman papillomavirus type 16 (HPV16) is the primary etiologic agent for cervical cancer. The infectious entry of HPV16 into cells occurs via a so-far poorly characterized clathrin-and caveolin-independent endocytic pathway, which involves tetraspanin proteins and actin. In this study, we investigated the specific role of the tetraspanin CD151 in the early steps of HPV16 infection. We show that surface-bound HPV16 moves together with CD151 within the plane of the membrane before they cointernalize into endosomes. Depletion of endogenous CD151 did not affect binding of viral particles to cells but resulted in reduction of HPV16 endocytosis. HPV16 uptake is dependent on the C-terminal cytoplasmic region of CD151 but does not require its tyrosine-based sorting motif. Reexpression of the wild-type CD151 but not mutants affecting integrin functions restored virus internalization in CD151-depleted cells. Accordingly, short interfering RNA (siRNA) gene knockdown experiments confirmed that CD151-associated integrins (i.e., ␣3␤1 and ␣6␤1/4) are involved in HPV16 infection. Furthermore, palmitoylation-deficient CD151 did not support HPV16 cell entry. These data show that complex formation of CD151 with laminin-binding integrins and integration of the complex into tetraspanin-enriched microdomains are critical for HPV16 endocytosis.

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“…Consequently, tetraspanins play roles in a wide range of biological activities, such as fertilization, muscle formation and repair, generation of synaptic contacts at neuromuscular junctions, maintenance of skin integrity, and induction of immune responses (1)(2)(3)(4). They are also implicated in pathologies, including cancer (e.g., metastasis [5]) and inherited disorders (6), as well as in the propagation and pathogenesis of numerous infectious agents (parasites, bacteria, and viruses) (7)(8)(9)(10)(11).…”

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confidence: 99%

Vpu Is the Main Determinant for Tetraspanin Downregulation in HIV-1-Infected Cells

Lambelé

Koppensteiner

Symeonides

et al. 2015

J Virol

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Tetraspanins constitute a family of cellular proteins that organize various membrane-based processes. Several members of this family, including CD81, are actively recruited by HIV-1 Gag to viral assembly and release sites. Despite their enrichment at viral exit sites, the overall levels of tetraspanins are decreased in HIV-1-infected cells. Here, we identify Vpu as the main viral determinant for tetraspanin downregulation. We also show that reduction of CD81 levels by Vpu is not a by-product of CD4 or BST-2/ tetherin elimination from the surfaces of infected cells and likely occurs through an interaction between Vpu and CD81. Finally, we document that Vpu-mediated downregulation of CD81 from the surfaces of infected T cells can contribute to preserving the infectiousness of viral particles, thus revealing a novel Vpu function that promotes virus propagation by modulating the host cell environment. IMPORTANCEThe HIV-1 accessory protein Vpu has previously been shown to downregulate various host cell factors, thus helping the virus to overcome restriction barriers, evade immune attack, and maintain the infectivity of viral particles. Our study identifies tetraspanins as an additional group of host factors whose expression at the surfaces of infected cells is lowered by Vpu. While the downregulation of these integral membrane proteins, including CD81 and CD82, likely affects more than one function of HIV-1-infected cells, we document that Vpu-mediated lowering of CD81 levels in viral particles can be critical to maintaining their infectiousness. Tetraspanins are integral membrane proteins that span the lipid bilayer four times. The 33 members (in humans) of this protein family, by homo-and hetero-oligomerizing and by laterally interacting with other proteins and with lipids, form a web that serves as the basis for their involvement in the organization of membranes. When triggered by intra-or extracellular cues, socalled tetraspanin-enriched microdomains (TEMs) can form, and these platforms then support or modulate various membranebased processes, including cell adhesion, membrane fusion, signaling, and protein sorting. Consequently, tetraspanins play roles in a wide range of biological activities, such as fertilization, muscle formation and repair, generation of synaptic contacts at neuromuscular junctions, maintenance of skin integrity, and induction of immune responses (1-4). They are also implicated in pathologies, including cancer (e.g., metastasis [5]) and inherited disorders (6), as well as in the propagation and pathogenesis of numerous infectious agents (parasites, bacteria, and viruses) (7-11).While one member of the tetraspanin family (CD63) was shown more than 2 decades ago to be specifically acquired by HIV-1 particles released from infected cells (12)(13)(14), only during the past decade has work by several groups documented that tetraspanins play roles during different stages of the viral replication cycle (for recent reviews, see references 9 and 15). The tetraspanins CD9, CD53, CD63, CD81, CD...

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Tetraspanins - Gateways for Infection

Cited by 69 publications

References 209 publications

Tetraspanins at a glance

Tetraspanins at a glance

Tetraspanin CD151 Mediates Papillomavirus Type 16 Endocytosis

Vpu Is the Main Determinant for Tetraspanin Downregulation in HIV-1-Infected Cells

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