Glycoprotein G isoforms from some alphaherpesviruses function as broad-spectrum chemokine binding proteins.
Open accessAbstract
Mimicry of host chemokines and chemokine receptors to modulate chemokine activity is a strategy encoded by beta- and gammaherpesviruses, but very limited information is available on the anti-chemokine strategies encoded by alphaherpesviruses. The secretion of chemokine binding proteins (vCKBPs) has hitherto been considered a unique strategy encoded by poxviruses and gammaherpesviruses. We describe a family of novel vCKBPs in equine herpesvirus 1, bovine herpesvirus 1 and 5, and related alphaherpesviruses with no sequence similarity to chemokine receptors or other vCKBPs. We show that glycoprotein G (gG) is secreted from infected cells, binds a broad range of chemokines with high affinity and blocks chemokine activity by preventing their interaction with specific receptors. Moreover, gG also blocks chemokine binding to glycosaminoglycans, an interaction required for the correct presentation and function of chemokines in vivo. In contrast to other vCKBPs, gG may also be membrane anchored and, consistently, we show chemokine binding activity at the surface of cells expressing full-length protein. These alphaherpesvirus vCKBPs represent a novel family of proteins that bind chemokines both at the membrane and in solution.
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EHV-1 gG is a chemokine binding protein (vCKBP) that binds a broad range of chemokines, such as IL-8 and CXCL1, with high affinity and blocks their activity.
“EHV-1 gG is a chemokine binding protein (vCKBP), which binds to a broad range of chemokines, such as IL-8 and CXCL1, with high affinity and subsequently blocks their activity (Bryant et al., 2003).”
From The Pathogenesis and Immune Evasive Mechanisms of Equine Herpesvirus Type 1 (2021) · cites this paper as Bryant et al., 2003
The Discussion identifies EHV-1 gG as a high-affinity chemokine-binding protein, and Figure 4 documents CXCL1 binding. The biological-activity results (Figure 7) show EHV-1 gG inhibiting CXCL8 (IL-8)-induced neutrophil migration, but attribute inhibition of CXCL1-induced migration to BHV-1 gG, not EHV-1 gG. Thus the claim overstates the evidence if it says EHV-1 gG blocks the activity of both named chemokines. (LLM, conf=0.86)
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Self-citation
- Authors
- Bryant, N. A., Davis‐Poynter, N., Vanderplasschen, A., & Alcami, A.
- Affiliations
- University of Cambridge (GB)
- University of Liège (BE)
- Venue
- The EMBO Journal
- Published
- 2003-02-17
- Volume
- 22
- Issue
- 4
- Pages
- 833-846
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC145452
- OpenAlex
- W2092411293
- Cited by
- 141
- References
- 48
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 6 · 2023: 4 · 2022: 2 · 2021: 5 · 2020: 7 · 2019: 7 · 2018: 2 · 2017: 5 · 2016: 5 · 2015: 1 · 2014: 3 · 2013: 10 · 2012: 7
- FWCI
- 5.14
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- ORBi (University of Liège) (submittedVersion)
- Funders
- Wellcome Trust (051087/Z97/Z)
- Fédération Wallonie-Bruxelles
- Biotechnology and Biological Sciences Research Council
- Topics
- Health Sciences › Medicine › Epidemiology › Herpesvirus Infections and Treatments
- Health Sciences › Medicine › Oncology › Chemokine receptors and signaling
- Health Sciences › Medicine › Epidemiology › Cytomegalovirus and herpesvirus research
- Keywords
- alphaherpesvirus, glycoprotein G, chemokine binding protein, chemokine receptor antagonism, equine herpesvirus 1, bovine herpesvirus 1, bovine herpesvirus 5, glycosaminoglycan binding
- MeSH terms
- Amino Acid Sequence, Animals, Cattle, Herpesvirus 1, Equid, Heparin, Horses, Humans, Herpesvirus 1, Bovine, Molecular Sequence Data, Protein Binding, Viral Envelope Proteins, Viral Proteins, Cytokines, Sequence Alignment, Alphaherpesvirinae, Protein Isoforms, Herpesvirus 5, Bovine
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