7puy › Citations

Structure and receptor recognition by the Lassa virus spike complex.

Katz M, Weinstein J, Eilon-Ashkenazy M, Gehring K, Cohen-Dvashi H, Elad N, Fleishman SJ, Diskin R
Nature 603 174-179 (2022)
Cited: 14 times
EuropePMC logo PMID: 35173332

Abstract

Lassa virus (LASV) is a human pathogen, causing substantial morbidity and mortality1,2. Similar to other Arenaviridae, it presents a class-I spike complex on its surface that facilitates cell entry. The virus's cellular receptor is matriglycan, a linear carbohydrate that is present on α-dystroglycan3,4, but the molecular mechanism that LASV uses to recognize this glycan is unknown. In addition, LASV and other arenaviruses have a unique signal peptide that forms an integral and functionally important part of the mature spike5-8; yet the structure, function and topology of the signal peptide in the membrane remain uncertain9-11. Here we solve the structure of a complete native LASV spike complex, finding that the signal peptide crosses the membrane once and that its amino terminus is located in the extracellular region. Together with a double-sided domain-switching mechanism, the signal peptide helps to stabilize the spike complex in its native conformation. This structure reveals that the LASV spike complex is preloaded with matriglycan, suggesting the mechanism of binding and rationalizing receptor recognition by α-dystroglycan-tropic arenaviruses. This discovery further informs us about the mechanism of viral egress and may facilitate the rational design of novel therapeutics that exploit this binding site.

Articles - 7puy mentioned but not cited (3)

  1. research-article Defining bottlenecks and opportunities for Lassa virus neutralization by structural profiling of vaccine-induced polyclonal antibody responses. Brouwer PJM, Perrett HR, Beaumont T, Nijhuis H, Kruijer S, Burger JA, Lee WH, Müller-Kraüter H, Sanders RW, Strecker T, van Gils MJ, Ward AB. bioRxiv 2023.12.21.572918 (2023)
  2. Deletion of the first glycosylation site promotes Lassa virus glycoprotein-mediated membrane fusion. Dong S, Mao W, Liu Y, Jia X, Zhang Y, Zhou M, Hou Y, Xiao G, Wang W. Virol Sin 38 380-386 (2023)
  3. Screening and Identification of Lassa Virus Entry Inhibitors from a Fragment-Based Drug Discovery Library. Hou Y, Liu Y, Jia X, Zhou M, Mao W, Dong S, Zhang Y, Xiao G, Wang W. Viruses 14 2649 (2022)


Reviews citing this publication (1)

  1. Antiviral PROTACs: Opportunity borne with challenge. Liang J, Wu Y, Lan K, Dong C, Wu S, Li S, Zhou HB. Cell Insight 2 100092 (2023)

Articles citing this publication (10)

  1. Lassa virus glycoprotein nanoparticles elicit neutralizing antibody responses and protection. Brouwer PJM, Antanasijevic A, Ronk AJ, Müller-Kräuter H, Watanabe Y, Claireaux M, Perrett HR, Bijl TPL, Grobben M, Umotoy JC, Schriek AI, Burger JA, Tejjani K, Lloyd NM, Steijaert TH, van Haaren MM, Sliepen K, de Taeye SW, van Gils MJ, Crispin M, Strecker T, Bukreyev A, Ward AB, Sanders RW. Cell Host Microbe 30 1759-1772.e12 (2022)
  2. Neutralizing Antibodies against Lassa Virus Lineage I. Buck TK, Enriquez AS, Schendel SL, Zandonatti MA, Harkins SS, Li H, Moon-Walker A, Robinson JE, Branco LM, Garry RF, Saphire EO, Hastie KM. mBio 13 e0127822 (2022)
  3. A cocktail of protective antibodies subverts the dense glycan shield of Lassa virus. Li H, Buck T, Zandonatti M, Yin J, Moon-Walker A, Fang J, Koval A, Heinrich ML, Rowland MM, Diaz Avalos R, Schendel SL, Parekh D, Zyla D, Enriquez A, Harkins S, Sullivan B, Smith V, Chukwudozie O, Watanabe R, Robinson JE, Garry RF, Branco LM, Hastie KM, Saphire EO. Sci Transl Med 14 eabq0991 (2022)
  4. Cell surface glycan engineering reveals that matriglycan alone can recapitulate dystroglycan binding and function. Sheikh MO, Capicciotti CJ, Liu L, Praissman J, Ding D, Mead DG, Brindley MA, Willer T, Campbell KP, Moremen KW, Wells L, Boons GJ. Nat Commun 13 3617 (2022)
  5. Cleavage-intermediate Lassa virus trimer elicits neutralizing responses, identifies neutralizing nanobodies, and reveals an apex-situated site-of-vulnerability. Gorman J, Cheung CS, Duan Z, Ou L, Wang M, Chen X, Cheng C, Biju A, Sun Y, Wang P, Yang Y, Zhang B, Boyington JC, Bylund T, Charaf S, Chen SJ, Du H, Henry AR, Liu T, Sarfo EK, Schramm CA, Shen CH, Stephens T, Teng IT, Todd JP, Tsybovsky Y, Verardi R, Wang D, Wang S, Wang Z, Zheng CY, Zhou T, Douek DC, Mascola JR, Ho DD, Ho M, Kwong PD. Nat Commun 15 285 (2024)
  6. Host-Associated Distribution of Two Novel Mammarenaviruses in Rodents from Southern Africa. Geldenhuys M, Weyer J, Kearney T, Markotter W. Viruses 15 99 (2022)
  7. Lassa Virus Structural Biology and Replication. Garry RF. Curr Top Microbiol Immunol 440 147-164 (2023)
  8. Structural basis for matriglycan synthesis by the LARGE1 dual glycosyltransferase. Katz M, Diskin R. PLoS One 17 e0278713 (2022)
  9. Structural conservation of Lassa virus glycoproteins and recognition by neutralizing antibodies. Perrett HR, Brouwer PJM, Hurtado J, Newby ML, Liu L, Müller-Kräuter H, Müller Aguirre S, Burger JA, Bouhuijs JH, Gibson G, Messmer T, Schieffelin JS, Antanasijevic A, Boons GJ, Strecker T, Crispin M, Sanders RW, Briney B, Ward AB. Cell Rep 42 112524 (2023)
  10. Using Machine Learning Methods in Identifying Genes Associated with COVID-19 in Cardiomyocytes and Cardiac Vascular Endothelial Cells. Xu Y, Ma Q, Ren J, Chen L, Guo W, Feng K, Zeng Z, Huang T, Cai Y. Life (Basel) 13 1011 (2023)


Quick links