Canine and feline parvoviruses preferentially recognize the non-human cell surface sialic acid N-glycolylneuraminic acid

Löfling, Jonas; Lyi, Sangbom M.; Parrish, Colin R.; Varki, Ajit

doi:10.1016/j.virol.2013.02.009

Cited by 38 publications

(43 citation statements)

References 52 publications

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“…This changes the binding affinity of these receptors and permits several agents, which were blocked for infection during the breast‐feeding period now to bind, penetrate and to exert potentially pathogenic functions (e.g., Ref. ). Neu5Gc is not synthesized in chicken and either not found in fish or present there in a highly re‐arranged form.…”

Section: Protection Of Newborn Babies During Breast‐feeding Periodmentioning

confidence: 99%

Specific nutritional infections early in life as risk factors for human colon and breast cancers several decades later

Hausen

Bund

Villiers

2018

Intl Journal of Cancer

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Section: Protection Of Newborn Babies During Breast‐feeding Periodmentioning

confidence: 99%

Specific nutritional infections early in life as risk factors for human colon and breast cancers several decades later

Hausen

Bund

Villiers

2018

Intl Journal of Cancer

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“…For several members of the parvovirus genus, terminal SIA serves as a glycan receptor (Table 1), although for Canine Parvovirus (CPV) and Feline Panleukopenia Virus (FPV), SIA recognition is not essential for infection, but rather utilized during hemagglutination (HA) of erythrocytes [76]. CPV and FPV recognize both α2-3 and α2-6 linked N-glycolyl neuraminic acid, a non-human SIA.…”

Section: Glycans Receptor Utilization By the Autonomous Parvoviruses mentioning

confidence: 99%

Parvovirus glycan interactions

Huang

Halder

Agbandje‐McKenna

2014

Current Opinion in Virology

108

102

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Members of the Parvoviridae utilize glycan receptors for cellular attachment and subsequent interactions determine transduction efficiency or pathogenic outcome. This review focuses on the identity of the glycan receptors utilized, their capsid binding footprints, and a discussion of the overlap of these sites with tropism, transduction, and pathogenicity determinants. Despite high sequence diversity between the different genera, most parvoviruses bind to negatively charged glycans, such as sialic acid and heparan sulfate, abundant on cell surface membranes. The capsid structure of these viruses exhibit high structural homology enabling common regions to be utilized for glycan binding and at the same time the sequence diversity at the common footprints allows for binding of different glycans or differential binding of the same glycan.

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“…The capsid binds transferrin receptor type 1 (TfR), and TfR is the essential and apparently only receptor required by CPV and its relatives for binding to and infection of carnivore host cells (22,23). The capsid may also bind sialic acids, specifically the modified form N-glycolylneuraminic acid (Neu5Gc), which is present in some hosts but not others, and while that binding is not an essential receptor interaction, it may reduce the infectivity of cells (24). The capsid stimulates the formation of and is the target for host antibodies that efficiently block infection and aid in recovery from disease (25,26).…”

mentioning

confidence: 99%

Parvovirus Capsid Structures Required for Infection: Mutations Controlling Receptor Recognition and Protease Cleavages

Callaway

Feng

Lee

et al. 2017

J Virol

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Parvovirus capsids are small but complex molecular machines responsible for undertaking many of the steps of cell infection, genome packing, and cell-tocell as well as host-to-host transfer. The details of parvovirus infection of cells are still not fully understood, but the processes must involve small changes in the capsid structure that allow the endocytosed virus to escape from the endosome, pass through the cell cytoplasm, and deliver the single-stranded DNA (ssDNA) genome to the nucleus, where viral replication occurs. Here, we examine capsid substitutions that eliminate canine parvovirus (CPV) infectivity and identify how those mutations changed the capsid structure or altered interactions with the infectious pathway. Amino acid substitutions on the exterior surface of the capsid (Gly299Lys/Ala300Lys) altered the binding of the capsid to transferrin receptor type 1 (TfR), particularly during virus dissociation from the receptor, but still allowed efficient entry into both feline and canine cells without successful infection. These substitutions likely control specific capsid structural changes resulting from TfR binding required for infection. A second set of changes on the interior surface of the capsid reduced viral infectivity by Ͼ100-fold and included two cysteine residues and neighboring residues. One of these substitutions, Cys270Ser, modulates a VP2 cleavage event found in ϳ10% of the capsid proteins that also was shown to alter capsid stability. A neighboring substitution, Pro272Lys, significantly reduced capsid assembly, while a Cys273Ser change appeared to alter capsid transport from the nucleus. These mutants reveal additional structural details that explain cell infection processes of parvovirus capsids.IMPORTANCE Parvoviruses are commonly found in both vertebrate and invertebrate animals and cause widespread disease. They are also being developed as oncolytic therapeutics and as gene therapy vectors. Most functions involved in infection or transduction are mediated by the viral capsid, but the structure-function correlates of the capsids and their constituent proteins are still incompletely understood, especially in relation to identifying capsid processes responsible for infection and release from the cell. Here, we characterize the functional effects of capsid protein mutations that result in the loss of virus infectivity, giving a better understanding of the portions of the capsid that mediate essential steps in successful infection pathways and how they contribute to viral infectivity.

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Canine and feline parvoviruses preferentially recognize the non-human cell surface sialic acid N-glycolylneuraminic acid

Cited by 38 publications

References 52 publications

Specific nutritional infections early in life as risk factors for human colon and breast cancers several decades later

Specific nutritional infections early in life as risk factors for human colon and breast cancers several decades later

Parvovirus glycan interactions

Parvovirus Capsid Structures Required for Infection: Mutations Controlling Receptor Recognition and Protease Cleavages

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