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Anne Haywood

TitleAssociate Professor
InstitutionSchool of Medicine and Dentistry
DepartmentPediatrics
AddressUniversity of Rochester Medical Center
School of Medicine and Dentistry
601 Elmwood Ave, Box 777
Rochester NY 14642
Other Positions
TitleAssociate Professor
InstitutionSchool of Medicine and Dentistry
DepartmentMicrobiology and Immunology

 
 Overview
1) Entry of enveloped viruses
Viral entry includes viral binding to receptors, membrane fusion, uncoating and trafficking. My work on viral entry began by initiating the use of Sendai virus (murine parainfluenza virus type 1) with liposomes that contained a viral receptor in the membrane. This model system shows what steps in viral entry are primarily determined by virus components and gives a very simple system to search for new principles. The following new principles were found. 1) Sialic acids were long known to have receptor activity for parainfluenza and influenza viruses, but it was assumed viral receptors were sialoglycoproteins. With liposomes it was shown that gangliosides (sialoglycolipids) can also serve as receptors. 2) Binding occurs at temperatures as low as 0-4°C. Adding virus to liposomes containing gangliosides at 4°C and raising the temperature to 37°C causes the liposomes to envelope the bound viruses. Others followed this up by showing that circumferential binding also causes the initial step of phagocytosis by macrophages. 3) Sendai virus membranes fuse with ganglioside-containing liposomes. This shows that the virus directs fusion and only requires the host to present virus receptor. Further work showed that Sendai virus fuses at the leading edge of the area of the envelopment caused by receptor binding. The high curvature of the leading edge in the liposome membrane changes the membrane bilayer in ways that facilitate membrane fusion. 4) Influenza virus also fuses with liposomes containing gangliosides at neutral pH; whereas, it has been argued that influenza virus requires low pH to fuse its membrane. 5) "Uncoating" involves changes in a viral particle and release of the viral contents into the cell. Electron micrographs suggested that uncoating is an active process, whereas, previously it has been thought a passive result of fusion. A review of recent literature suggested that, when a virus particle is intact, uncoating is different from the generally used model derived in 1968 from experiments using damaged particles.

2) Persistent viral infections
Many viruses from different viral families can form a persistent infection. Viral persistence is more likely to occur if the infection is in the very young and especially in fetuses. Rubella virus is an example of a virus that forms a persistent infection. Rubella-infected fetuses continue to shed virus at birth and for months thereafter. The autopsies of fetuses with congenital rubella syndrome revealed that many tissues were infected. When cells derived from infected tissues were made into cell cultures, the cells were persistently infected. Some infants with congenital rubella syndrome have problems that show up after infancy. These include endocrine problems, late onset of loss of hearing, late onset of ocular problems and neurological problems, which include autism. Consideration of late occurring problems associated with a virus raises the question whether the persistent virus is present in low amounts and causing alterations in the affected organ or whether the virus could have altered the immune system, which then causes the pathology. Some women who accidentally received rubella vaccine during pregnancy had infants who shed vaccine virus at and beyond birth. Thus rubella vaccine virus retained the ability to form a persistent infection, although the multiple viral mutations involved in attenuation changes the infection. For some persistent virus infections a mother who was infected previously can infect her infant in utero. For some other persistent viruses, like rubella, it has not been shown whether the virus can persist long enough so that it could cause infection of the placenta and fetus if the mother became pregnant considerably after the infection. Such an infection might perhaps first express itself clinically as one of the later complications.

 
 Selected Publications
List All   |   Timeline
  1. Haywood AM. Membrane uncoating of intact enveloped viruses. J Virol. 2010 Nov; 84(21):10946-55.
    View in: PubMed
  2. Haywood AM. Transmissible spongiform encephalopathies. N Engl J Med. 1997 Dec 18; 337(25):1821-8.
    View in: PubMed
  3. Haywood AM. Virus receptors: binding, adhesion strengthening, and changes in viral structure. J Virol. 1994 Jan; 68(1):1-5.
    View in: PubMed
  4. Haywood AM. Relationships between binding, phagocytosis and membrane fusion of enveloped viruses. Prog Clin Biol Res. 1990; 343:117-32.
    View in: PubMed
  5. Haywood AM, Boyer BP. Time and temperature dependence of influenza virus membrane fusion at neutral pH. J Gen Virol. 1986 Dec; 67 ( Pt 12):2813-7.
    View in: PubMed
  6. Haywood AM. Patterns of persistent viral infections. N Engl J Med. 1986 Oct 9; 315(15):939-48.
    View in: PubMed
  7. Haywood AM, Boyer BP. Ficoll and dextran enhance adhesion of Sendai virus to liposomes containing receptor (ganglioside GD1a). Biochemistry. 1986 Jul 1; 25(13):3925-9.
    View in: PubMed
  8. Haywood AM, Boyer BP. Fusion of influenza virus membranes with liposomes at pH 7.5. Proc Natl Acad Sci U S A. 1985 Jul; 82(14):4611-5.
    View in: PubMed
  9. Haywood AM, Boyer BP. Effect of lipid composition upon fusion of liposomes with Sendai virus membranes. Biochemistry. 1984 Aug 28; 23(18):4161-6.
    View in: PubMed
  10. Haywood AM, Boyer BP. Sendai virus membrane fusion: time course and effect of temperature, pH, calcium, and receptor concentration. Biochemistry. 1982 Nov 23; 21(24):6041-6.
    View in: PubMed
  11. Haywood AM, Boyer BP. Fusion and disassembly of sendai virus membranes with liposomes. Biophys J. 1982 Jan; 37(1):128-30.
    View in: PubMed
  12. Haywood AM, Boyer BP. Initiation of fusion and disassembly of Sendai virus membranes into liposomes. Biochim Biophys Acta. 1981 Aug 6; 646(1):31-5.
    View in: PubMed
  13. Haywood AM. Interactions of liposomes with viruses. Ann N Y Acad Sci. 1978; 308:275-80.
    View in: PubMed
  14. Haywood AM. 'Phagocytosis' of sendai virus by model membranes. J Gen Virol. 1975 Oct; 29(1):63-8.
    View in: PubMed
  15. Haywood AM. Letter to the editor: Fusion of Sendai viruses with model membranes. J Mol Biol. 1974 Aug 15; 87(3):625-8.
    View in: PubMed
  16. Haywood AM. Characteristics of Sendai virus receptors in a model membrane. J Mol Biol. 1974 Mar 15; 83(4):427-36.
    View in: PubMed
  17. Ricciuti CP, Haywood AM. Production of defective MS2 virions in resting Escherichia coli. Virology. 1974 Mar; 58(1):164-75.
    View in: PubMed
  18. Haywood AM. Two classes of membrane binding of replicative RNA of bacteriophage MS2. Proc Natl Acad Sci U S A. 1973 Aug; 70(8):2381-5.
    View in: PubMed
  19. Haywood AM, McClellen RE. Ribosomal ribonucleic acid maturation and synthesis after ribonucleic acid bacteriophage infection. Biochemistry. 1973 Jul 17; 12(15):2905-9.
    View in: PubMed
  20. Pierce JS, Haywood AM. Thermal inactivation of Newcastle disease virus. I. Coupled inactivation rates of hemagglutinating and neuraminidase activities. J Virol. 1973 Feb; 11(2):168-76.
    View in: PubMed
  21. Haywood AM. Cellular site of Escherichia coli ribosomal RNA synthesis. Proc Natl Acad Sci U S A. 1971 Feb; 68(2):435-9.
    View in: PubMed
  22. Haywood AM, Cramer JH, Shoemaker NL. Host-virus interaction in ribonucleic acid bacteriophage-infected Escherichia coli. I. Location of "late" MS2-specific ribonucleic acid synthesis. J Virol. 1969 Oct; 4(4):364-71.
    View in: PubMed
  23. Haywood AM, Harris JM. Actinomycin inhibition of MS2 replication. J Mol Biol. 1966 Jul; 18(3):448-63.
    View in: PubMed
  24. Haywood AM, Sinsheimer RL. The replication of bacteriophage MS2. V. Proteins specifically associated with infection. J Mol Biol. 1965 Dec; 14(2):305-26.
    View in: PubMed
  25. HAYWOOD AM, SINSHEIMER RL. Inhibition of protein synthesis in E. coli protoplasts by actinomycin-D. J Mol Biol. 1963 Mar; 6:247-9.
    View in: PubMed

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