Serum amyloid P component inhibits influenza A virus infections: in vitro and in vivo studies.

A Horvath; I Andersen; K Junker; B Lyck Fogh-Schultz; E Holm Nielsen; S Gizurarson; Ove Andersen; J Karman; E Rajnavolgyi; A Erdei; SE Svehag

doi:http://dx.doi.org/10.1016/S0166-3542(01)00158-9

Serum amyloid P component inhibits influenza A virus infections: in vitro and in vivo studies.

A Horvath, I Andersen, K Junker, B Lyck Fogh-Schultz, E Holm Nielsen, S Gizurarson, Ove Andersen, J Karman, E Rajnavolgyi, A Erdei, SE Svehag

26 Citations (Scopus)

Abstract

Serum amyloid P component (SAP) binds in vitro Ca(2+)-dependently to several ligands including oligosaccharides with terminal mannose and galactose. We have earlier reported that SAP binds to human influenza A virus strains, inhibiting hemagglutinin (HA) activity and virus infectivity in vitro. These studies were extended to comprise five mouse-adapted influenza A strains, two swine influenza A strains, a mink influenza A virus, a ferret influenza A reassortant virus, a influenza B virus and a parainfluenza 3 virus. The HA activity of all these viruses was inhibited by SAP. Western blotting showed that SAP bound to HA trimers, monomers and HA1 and HA2 subunits of influenza A virus. Binding studies indicated that galactose, mannose and fucose moieties contributed to the SAP reacting site(s). Intranasal administration of human SAP to mice induced no demonstrable toxic reactions, and circulating antibodies against SAP were not detected. Preincubation of virus (A/Japan/57) with SAP prevented primary infection of mice and development of antiviral antibodies. After a single intranasal administration of SAP (40 microg) 1 h before primary infection with virus (2LD(50)), nine out of 10 mice survived on day 10 and these mice approached normal body weight, whereas control mice (one out of five surviving on day 10) died. The data provide evidence of the potential of intranasally administered SAP for prophylactic treatment of influenza A virus infections in humans.

Original language	English
Journal	Antiviral Research
Volume	52
Issue number	1
Pages (from-to)	43-53
ISSN	0166-3542
DOIs	https://doi.org/10.1016/S0166-3542(01)00158-9
Publication status	Published - 2001

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@article{27a0463d68e0469fa6109ae491d15e0c,

title = "Serum amyloid P component inhibits influenza A virus infections: in vitro and in vivo studies.",

abstract = "Serum amyloid P component (SAP) binds in vitro Ca(2+)-dependently to several ligands including oligosaccharides with terminal mannose and galactose. We have earlier reported that SAP binds to human influenza A virus strains, inhibiting hemagglutinin (HA) activity and virus infectivity in vitro. These studies were extended to comprise five mouse-adapted influenza A strains, two swine influenza A strains, a mink influenza A virus, a ferret influenza A reassortant virus, a influenza B virus and a parainfluenza 3 virus. The HA activity of all these viruses was inhibited by SAP. Western blotting showed that SAP bound to HA trimers, monomers and HA1 and HA2 subunits of influenza A virus. Binding studies indicated that galactose, mannose and fucose moieties contributed to the SAP reacting site(s). Intranasal administration of human SAP to mice induced no demonstrable toxic reactions, and circulating antibodies against SAP were not detected. Preincubation of virus (A/Japan/57) with SAP prevented primary infection of mice and development of antiviral antibodies. After a single intranasal administration of SAP (40 microg) 1 h before primary infection with virus (2LD(50)), nine out of 10 mice survived on day 10 and these mice approached normal body weight, whereas control mice (one out of five surviving on day 10) died. The data provide evidence of the potential of intranasally administered SAP for prophylactic treatment of influenza A virus infections in humans.",

author = "A Horvath and I Andersen and K Junker and {Lyck Fogh-Schultz}, B and {Holm Nielsen}, E and S Gizurarson and Ove Andersen and J Karman and E Rajnavolgyi and A Erdei and SE Svehag",

year = "2001",

doi = "http://dx.doi.org/10.1016/S0166-3542(01)00158-9",

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T1 - Serum amyloid P component inhibits influenza A virus infections: in vitro and in vivo studies.

AU - Horvath, A

AU - Andersen, I

AU - Junker, K

AU - Lyck Fogh-Schultz, B

AU - Holm Nielsen, E

AU - Gizurarson, S

AU - Andersen, Ove

AU - Karman, J

AU - Rajnavolgyi, E

AU - Erdei, A

AU - Svehag, SE

PY - 2001

Y1 - 2001

N2 - Serum amyloid P component (SAP) binds in vitro Ca(2+)-dependently to several ligands including oligosaccharides with terminal mannose and galactose. We have earlier reported that SAP binds to human influenza A virus strains, inhibiting hemagglutinin (HA) activity and virus infectivity in vitro. These studies were extended to comprise five mouse-adapted influenza A strains, two swine influenza A strains, a mink influenza A virus, a ferret influenza A reassortant virus, a influenza B virus and a parainfluenza 3 virus. The HA activity of all these viruses was inhibited by SAP. Western blotting showed that SAP bound to HA trimers, monomers and HA1 and HA2 subunits of influenza A virus. Binding studies indicated that galactose, mannose and fucose moieties contributed to the SAP reacting site(s). Intranasal administration of human SAP to mice induced no demonstrable toxic reactions, and circulating antibodies against SAP were not detected. Preincubation of virus (A/Japan/57) with SAP prevented primary infection of mice and development of antiviral antibodies. After a single intranasal administration of SAP (40 microg) 1 h before primary infection with virus (2LD(50)), nine out of 10 mice survived on day 10 and these mice approached normal body weight, whereas control mice (one out of five surviving on day 10) died. The data provide evidence of the potential of intranasally administered SAP for prophylactic treatment of influenza A virus infections in humans.

AB - Serum amyloid P component (SAP) binds in vitro Ca(2+)-dependently to several ligands including oligosaccharides with terminal mannose and galactose. We have earlier reported that SAP binds to human influenza A virus strains, inhibiting hemagglutinin (HA) activity and virus infectivity in vitro. These studies were extended to comprise five mouse-adapted influenza A strains, two swine influenza A strains, a mink influenza A virus, a ferret influenza A reassortant virus, a influenza B virus and a parainfluenza 3 virus. The HA activity of all these viruses was inhibited by SAP. Western blotting showed that SAP bound to HA trimers, monomers and HA1 and HA2 subunits of influenza A virus. Binding studies indicated that galactose, mannose and fucose moieties contributed to the SAP reacting site(s). Intranasal administration of human SAP to mice induced no demonstrable toxic reactions, and circulating antibodies against SAP were not detected. Preincubation of virus (A/Japan/57) with SAP prevented primary infection of mice and development of antiviral antibodies. After a single intranasal administration of SAP (40 microg) 1 h before primary infection with virus (2LD(50)), nine out of 10 mice survived on day 10 and these mice approached normal body weight, whereas control mice (one out of five surviving on day 10) died. The data provide evidence of the potential of intranasally administered SAP for prophylactic treatment of influenza A virus infections in humans.

U2 - http://dx.doi.org/10.1016/S0166-3542(01)00158-9

DO - http://dx.doi.org/10.1016/S0166-3542(01)00158-9

M3 - Journal article

SN - 0166-3542

VL - 52

SP - 43

EP - 53

JO - Antiviral Research

JF - Antiviral Research

IS - 1

ER -

Serum amyloid P component inhibits influenza A virus infections: in vitro and in vivo studies.

Abstract

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