The Intracellular Cargo Receptor ERGIC-53 Is Required for the Production of Infectious Arenavirus, Coronavirus, and Filovirus Particles

Klaus, Joseph P.; Eisenhauer, Philip; Russo, Joanne; Mason, Anne B.; Danh, C.; King, Benjamin R.; Taatjes, Douglas J.; Cornillez-Ty, Cromwell; Boyson, Jonathan E.; Thali, Markus; Zheng, Chunlei; Liao, Lujian; Yates, John R.; Zhang, Bin; Ballif, Bryan A.; Botten, Jason

doi:10.1016/j.chom.2013.10.010

Cited by 66 publications

(74 citation statements)

References 38 publications

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“…The GPC precursor is trafficked from the endoplasmic reticulum to the Golgi, where it is heavily N-glycosylated and processed by cellular proteases [signal peptidase (SPase) SKI1/SP1] into its mature form, which comprises noncovalently linked GP1, GP2, and SSP (18). GPC must also interact with ERGIC-53 in the exocytic pathway in order to form infectious virions (19). …”

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confidence: 99%

Structural basis for antibody-mediated neutralization of Lassa virus

Hastie

Zandonatti

Kleinfelter

et al. 2017

Science

185

335

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The arenavirus Lassa causes severe hemorrhagic fever and a significant disease burden in West Africa every year. The glycoprotein, GPC, is the sole antigen expressed on the viral surface and the critical target for antibody-mediated neutralization. Here we present the crystal structure of the trimeric, prefusion ectodomain of Lassa GP bound to a neutralizing antibody from a human survivor at 3.2-angstrom resolution. The antibody extensively anchors two monomers together at the base of the trimer, and biochemical analysis suggests that it neutralizes by inhibiting conformational changes required for entry. This work illuminates pH-driven conformational changes in both receptor-binding and fusion subunits of Lassa virus, illustrates the unique assembly of the arenavirus glycoprotein spike, and provides a much-needed template for vaccine design against these threats to global health.

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confidence: 99%

Structural basis for antibody-mediated neutralization of Lassa virus

Hastie

Zandonatti

Kleinfelter

et al. 2017

Science

185

335

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“…There is growing evidence that ERGIC-53 is closely related with virus infection. ERGIC-53 is required for the production of infectious arenavirus, coronavirus, and filovirus particles [11]. In the present study, a LTL (named PcL-lectin) was identified from red swamp crayfish, Procambarus clarkii.…”

Section: Introductionmentioning

confidence: 80%

A novel L-type lectin was required for the multiplication of WSSV in red swamp crayfish (Procambarus clakii)

Dai

Wang

Zhao

et al. 2016

Fish & Shellfish Immunology

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L-type lectins are involved in glycoproteins secretory pathways and are associated with many immune responses. There is growing evidence that L-type lectins are also involved in viral replication. In this study, a novel L-type lectin (named as PcL-lectin) was identified from red swamp crayfish (Procambarus clakii). Gene sequencing and phylogenetic tree analysis results showed that the PcL-lectin was a kind of endoplasmic reticulum Golgi intermediate compartment-53 (ERGIC-53). The expression level of PcL-lectin was significantly down regulated in crayfish after challenged with white spot syndrome virus (WSSV). Recombinant PcL-lectin protein facilitated the replication of WSSV in crayfish. In addition, WSSV replication was decreased when endogenous PcL-lectin was knocked down by RNA interference in crayfish. Furthermore, PcL-lectin may interact with VP24, an envelope protein of WSSV. Our results suggest that PcL-lectin may be required for the multiplication of WSSV, and will pave a new way for the developing of strategies against WSSV infection.

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“…In this issue, Klaus et al (2013) identify the cargo receptor endoplasmic reticulum (ER)-Golgi intermediate compartment 53 kDa protein (ERGIC-53) as a binding partner for viral GPs and a crucial cellular factor required for infectious virus production. In this issue, Klaus et al (2013) identify the cargo receptor endoplasmic reticulum (ER)-Golgi intermediate compartment 53 kDa protein (ERGIC-53) as a binding partner for viral GPs and a crucial cellular factor required for infectious virus production.…”

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confidence: 99%

“…In this issue of Cell Host & Microbe, Klaus et al (2013) sought to close this gap by performing a broad proteomic screen to identify cellular proteins that interact with viral envelope GPs. Enveloped viruses hijack the host cell's secretory pathway for GP biosynthesis.…”

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confidence: 99%