High-dose mannose-binding lectin therapy for Ebola virus infection

Ian C. Michelow; Calli Lear; Corinne Scully; Laura I. Prugar; Clifford B. Longley; L. Michael Yantosca; Xin Ji; Marshall Karpel; Matthew Brudner; Kazue Takahashi; Gregory T. Spear; R. Alan B. Ezekowitz; Emmett V. Schmidt; Gene G. Olinger

doi:10.1093/infdis/jiq025

High-dose mannose-binding lectin therapy for Ebola virus infection

Ian C. Michelow, Calli Lear, Corinne Scully, Laura I. Prugar, Clifford B. Longley, L. Michael Yantosca, Xin Ji, Marshall Karpel, Matthew Brudner, Kazue Takahashi, Gregory T. Spear, R. Alan B. Ezekowitz, Emmett V. Schmidt, Gene G. Olinger

Research output: Contribution to journal › Article › peer-review

Abstract

Mannose-binding lectin (MBL) targets diverse microorganisms for phagocytosis and complement-mediated lysis by binding specific surface glycans. Although recombinant human MBL (rhMBL) trials have focused on reconstitution therapy, safety studies have identified no barriers to its use at higher levels. Ebola viruses cause fatal hemorrhagic fevers for which no treatment exists and that are feared as potential biothreat agents. We found that mice whose rhMBL serum concentrations were increased ≥7-fold above average human levels survived otherwise fatal Ebola virus infections and became immune to virus rechallenge. Because Ebola glycoproteins potentially model other glycosylated viruses, rhMBL may offer a novel broadspectrum antiviral approach.

Original language	English (US)
Pages (from-to)	175-179
Number of pages	5
Journal	Journal of Infectious Diseases
Volume	203
Issue number	2
DOIs	https://doi.org/10.1093/infdis/jiq025
State	Published - Jan 15 2011
Externally published	Yes

ASJC Scopus subject areas

General Medicine

Access to Document

10.1093/infdis/jiq025

Cite this

@article{bb395f086c454c9f84111273f6c5fd5a,

title = "High-dose mannose-binding lectin therapy for Ebola virus infection",

abstract = "Mannose-binding lectin (MBL) targets diverse microorganisms for phagocytosis and complement-mediated lysis by binding specific surface glycans. Although recombinant human MBL (rhMBL) trials have focused on reconstitution therapy, safety studies have identified no barriers to its use at higher levels. Ebola viruses cause fatal hemorrhagic fevers for which no treatment exists and that are feared as potential biothreat agents. We found that mice whose rhMBL serum concentrations were increased ≥7-fold above average human levels survived otherwise fatal Ebola virus infections and became immune to virus rechallenge. Because Ebola glycoproteins potentially model other glycosylated viruses, rhMBL may offer a novel broadspectrum antiviral approach.",

author = "Michelow, {Ian C.} and Calli Lear and Corinne Scully and Prugar, {Laura I.} and Longley, {Clifford B.} and Yantosca, {L. Michael} and Xin Ji and Marshall Karpel and Matthew Brudner and Kazue Takahashi and Spear, {Gregory T.} and Ezekowitz, {R. Alan B.} and Schmidt, {Emmett V.} and Olinger, {Gene G.}",

year = "2011",

month = jan,

day = "15",

doi = "10.1093/infdis/jiq025",

language = "English (US)",

volume = "203",

pages = "175--179",

journal = "Journal of Infectious Diseases",

issn = "0022-1899",

publisher = "Oxford University Press",

number = "2",

}

TY - JOUR

T1 - High-dose mannose-binding lectin therapy for Ebola virus infection

AU - Michelow, Ian C.

AU - Lear, Calli

AU - Scully, Corinne

AU - Prugar, Laura I.

AU - Longley, Clifford B.

AU - Yantosca, L. Michael

AU - Ji, Xin

AU - Karpel, Marshall

AU - Brudner, Matthew

AU - Takahashi, Kazue

AU - Spear, Gregory T.

AU - Ezekowitz, R. Alan B.

AU - Schmidt, Emmett V.

AU - Olinger, Gene G.

PY - 2011/1/15

Y1 - 2011/1/15

N2 - Mannose-binding lectin (MBL) targets diverse microorganisms for phagocytosis and complement-mediated lysis by binding specific surface glycans. Although recombinant human MBL (rhMBL) trials have focused on reconstitution therapy, safety studies have identified no barriers to its use at higher levels. Ebola viruses cause fatal hemorrhagic fevers for which no treatment exists and that are feared as potential biothreat agents. We found that mice whose rhMBL serum concentrations were increased ≥7-fold above average human levels survived otherwise fatal Ebola virus infections and became immune to virus rechallenge. Because Ebola glycoproteins potentially model other glycosylated viruses, rhMBL may offer a novel broadspectrum antiviral approach.

AB - Mannose-binding lectin (MBL) targets diverse microorganisms for phagocytosis and complement-mediated lysis by binding specific surface glycans. Although recombinant human MBL (rhMBL) trials have focused on reconstitution therapy, safety studies have identified no barriers to its use at higher levels. Ebola viruses cause fatal hemorrhagic fevers for which no treatment exists and that are feared as potential biothreat agents. We found that mice whose rhMBL serum concentrations were increased ≥7-fold above average human levels survived otherwise fatal Ebola virus infections and became immune to virus rechallenge. Because Ebola glycoproteins potentially model other glycosylated viruses, rhMBL may offer a novel broadspectrum antiviral approach.

UR - http://www.scopus.com/inward/record.url?scp=79851506525&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79851506525&partnerID=8YFLogxK

U2 - 10.1093/infdis/jiq025

DO - 10.1093/infdis/jiq025

M3 - Article

C2 - 21288816

AN - SCOPUS:79851506525

SN - 0022-1899

VL - 203

SP - 175

EP - 179

JO - Journal of Infectious Diseases

JF - Journal of Infectious Diseases

IS - 2

ER -

High-dose mannose-binding lectin therapy for Ebola virus infection

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this