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Article ; Online: Opportunities, Technology, and the Joy of Discovery.

Spear, Patricia G

2022 Volume 9, Issue 1, Page(s) 1–17

Abstract: My grandparents were immigrants. My paternal grandfather was illiterate. Yet my parents were able to complete college and to become teachers. I had a conventional upbringing in a small town in Florida, graduating from high school in 1960. I was fortunate ...

Abstract	My grandparents were immigrants. My paternal grandfather was illiterate. Yet my parents were able to complete college and to become teachers. I had a conventional upbringing in a small town in Florida, graduating from high school in 1960. I was fortunate enough to graduate cum laude from Florida State University and to earn other credentials leading to faculty positions at outstanding institutions of higher education: the University of Chicago and Northwestern University. At a time when women were rarely the leaders of research groups, I was able to establish a well-funded research program and to make contributions to our understanding of viral entry into cells. My best research was done after I became confident enough to seek productive interactions with collaborators. I am grateful for the collaborators and collaborations that moved our field forward and for my trainees who have gone on to successes in many different careers.
MeSH term(s)	Female ; Humans ; Technology ; Universities
Language	English
Publishing date	2022-04-01
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2764224-0
ISSN	2327-0578 ; 2327-056X
ISSN (online)	2327-0578
ISSN	2327-056X
DOI	10.1146/annurev-virology-100520-012840
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Article ; Online: The Effect of Catheter Length Placed Into the Vein on Peripheral Ultrasound-Guided Catheter Survival Time: A Prospective Observational Study.

Miles, Gayla / Newcomb, Patricia / Spear, Dave

Journal of emergency nursing

2020 Volume 47, Issue 1, Page(s) 123–130

Abstract: Introduction: Establishing and maintaining peripheral intravenous access in patients with no visible or palpable veins can be arduous. Intravenous catheters placed with ultrasound do not survive as long as traditionally placed catheters. This study was ... ...

Abstract	Introduction: Establishing and maintaining peripheral intravenous access in patients with no visible or palpable veins can be arduous. Intravenous catheters placed with ultrasound do not survive as long as traditionally placed catheters. This study was performed to determine the relationship between the catheter length placed into the lumen of the vein using ultrasound and catheter survival. Methods: This was a nonrandomized prospective observational study of admitted patients with difficult intravenous placement in 2017. Subjects had ultrasound-guided peripheral intravenous placement in the emergency department or intensive care unit. The main outcome was the time of catheter survival. Data were analyzed using descriptive statistics and Cox regression. Results: A total of 98 patients with an average age of 63 years were enrolled. The total number of cases examined was 97 (N = 97), of which 29 intravenous catheters were removed for catheter-related problems (events). The mean (SD) survival time for catheters placed using ultrasound was 3,445 minutes (2,414) or 2.39 days. Peripheral catheter survival was not significantly related to the in-vein length of the catheter (X Discussion: The survival time of ultrasound-guided intravenous access doubled in the present study from 1674 minutes in a previous 2013 study. The results may have been due to clinician expertise and experience with the peripheral ultrasound-guided method and the use of updated equipment.
MeSH term(s)	Aged ; Catheterization, Peripheral/instrumentation ; Catheterization, Peripheral/nursing ; Device Removal ; Emergency Service, Hospital ; Female ; Humans ; Male ; Middle Aged ; Prospective Studies ; Texas ; Time Factors ; Ultrasonography, Interventional
Language	English
Publishing date	2020-09-23
Publishing country	United States
Document type	Journal Article ; Observational Study
ZDB-ID	604632-0
ISSN	1527-2966 ; 0099-1767
ISSN (online)	1527-2966
ISSN	0099-1767
DOI	10.1016/j.jen.2020.05.015
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Article: Herpes simplex virus: receptors and ligands for cell entry.

Spear, Patricia G

Cellular microbiology

2004 Volume 6, Issue 5, Page(s) 401–410

Abstract: Entry of herpes simplex virus (HSV) into cells depends upon multiple cell surface receptors and multiple proteins on the surface of the virion. The cell surface receptors include heparan sulphate chains on cell surface proteoglycans, a member of the ... ...

Abstract	Entry of herpes simplex virus (HSV) into cells depends upon multiple cell surface receptors and multiple proteins on the surface of the virion. The cell surface receptors include heparan sulphate chains on cell surface proteoglycans, a member of the tumor necrosis factor (TNF) receptor family and two members of the immunoglobulin superfamily related to the poliovirus receptor. The HSV ligands for these receptors are the envelope glycoproteins gB and gC for heparan sulphate and gD for the protein receptors and specific sites in heparan sulphate generated by certain 3-O-sulfotransferases. HSV gC also binds to the C3b component of complement and can block complement-mediated neutralization of virus. The purposes of this review are to summarize available information about these cell surface receptors and the viral ligands, gC and gD, and to discuss roles of these viral glycoproteins in immune evasion and cellular responses as well as in viral entry.
MeSH term(s)	Binding Sites ; Heparitin Sulfate/metabolism ; Humans ; Ligands ; Membrane Fusion ; Models, Molecular ; Protein Conformation ; Receptors, Virus/metabolism ; Simplexvirus/genetics ; Simplexvirus/metabolism ; Simplexvirus/pathogenicity ; Viral Envelope Proteins/chemistry ; Viral Envelope Proteins/genetics ; Viral Envelope Proteins/metabolism
Chemical Substances	Ligands ; Receptors, Virus ; Viral Envelope Proteins ; Heparitin Sulfate (9050-30-0)
Language	English
Publishing date	2004-05
Publishing country	England
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	1468320-9
ISSN	1462-5822 ; 1462-5814
ISSN (online)	1462-5822
ISSN	1462-5814
DOI	10.1111/j.1462-5822.2004.00389.x
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Article: Viral interactions with receptors in cell junctions and effects on junctional stability.

Spear, Patricia G

Developmental cell

2002 Volume 3, Issue 4, Page(s) 462–464

Abstract: Several viruses can use, as entry receptors, cell adhesion molecules that localize to junctional complexes of epithelial cells and other cell types. A recent publication in Cell describes how adenovirus can disrupt cell junctions, thereby effecting its ... ...

Abstract	Several viruses can use, as entry receptors, cell adhesion molecules that localize to junctional complexes of epithelial cells and other cell types. A recent publication in Cell describes how adenovirus can disrupt cell junctions, thereby effecting its release from basal surfaces of an infected epithelium to the apical or external environment.
MeSH term(s)	Animals ; Cell Adhesion Molecules/physiology ; Humans ; Intercellular Junctions/physiology ; Intercellular Junctions/virology ; Receptors, Virus/physiology ; Virus Replication/physiology
Chemical Substances	Cell Adhesion Molecules ; Receptors, Virus
Language	English
Publishing date	2002-10-31
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2054967-2
ISSN	1878-1551 ; 1534-5807
ISSN (online)	1878-1551
ISSN	1534-5807
DOI	10.1016/s1534-5807(02)00298-8
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Article: Random linker-insertion mutagenesis to identify functional domains of herpes simplex virus type 1 glycoprotein B.

Lin, Erick / Spear, Patricia G

Proceedings of the National Academy of Sciences of the United States of America

2007 Volume 104, Issue 32, Page(s) 13140–13145

Abstract: Herpes simplex virus glycoprotein B (gB) is one of four glycoproteins essential for viral entry and cell fusion. Recently, an x-ray structure of the nearly full-length trimeric gB ectodomain was determined. Five structural domains and two linker regions ... ...

Abstract	Herpes simplex virus glycoprotein B (gB) is one of four glycoproteins essential for viral entry and cell fusion. Recently, an x-ray structure of the nearly full-length trimeric gB ectodomain was determined. Five structural domains and two linker regions were identified in what is probably a postfusion conformation. To identify functional domains of gB, we performed random linker-insertion mutagenesis. Analyses of 81 mutants revealed that only 27 could fold to permit processing and transport of gB to the cell surface. These 27 mutants fell into three categories. Insertions into two regions excluded from the solved structure (the N terminus and the C-terminal cytoplasmic tail) had no negative effect on cell fusion and viral entry activity, identifying regions that can tolerate altered structure without loss of function. Insertions into a disordered region in domain II and the adjacent linker region also permitted partial cell fusion and viral entry activity. Insertions at 16 other positions resulted in loss of cell fusion and viral entry activity, despite detectable levels of cell surface expression. Four of these insertion sites were not included in the solved structure. Two were between residues exposed to a cavity that is too small to accommodate the 5-amino acid insertions, consistent with the solved structure being different from the native prefusion structure. Ten were between residues exposed to the surface of the trimer, identifying regions that may be critical for interactions with other viral proteins or cellular components or for transitions from the prefusion to postfusion state.
MeSH term(s)	Animals ; CHO Cells ; Cricetinae ; Cricetulus ; Membrane Fusion ; Membrane Glycoproteins/chemistry ; Membrane Glycoproteins/physiology ; Mutagenesis, Insertional ; Protein Structure, Tertiary ; Structure-Activity Relationship ; Viral Envelope Proteins/chemistry ; Viral Envelope Proteins/physiology
Chemical Substances	G protein, vesicular stomatitis virus ; Membrane Glycoproteins ; Viral Envelope Proteins ; glycoprotein B, Simplexvirus
Language	English
Publishing date	2007-08-07
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.0705926104
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Article ; Online: Biochemistry. Viral glycoproteins and an evolutionary conundrum.

Steven, Alasdair C / Spear, Patricia G

Science (New York, N.Y.)

2006 Volume 313, Issue 5784, Page(s) 177–178

MeSH term(s)	Bacteriophages/chemistry ; Bacteriophages/genetics ; Capsid Proteins/chemistry ; Crystallography, X-Ray ; Evolution, Molecular ; Genome, Viral ; Herpesvirus 1, Human/chemistry ; Herpesvirus 1, Human/genetics ; Hydrogen-Ion Concentration ; Membrane Glycoproteins/chemistry ; Membrane Glycoproteins/genetics ; Models, Molecular ; Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Vesicular stomatitis Indiana virus/chemistry ; Vesicular stomatitis Indiana virus/genetics ; Viral Envelope Proteins/chemistry ; Viral Envelope Proteins/genetics ; Viral Fusion Proteins/chemistry ; Viral Fusion Proteins/genetics
Chemical Substances	Capsid Proteins ; G protein, vesicular stomatitis virus ; Membrane Glycoproteins ; Protein Subunits ; Viral Envelope Proteins ; Viral Fusion Proteins ; glycoprotein B, Simplexvirus
Language	English
Publishing date	2006-07-14
Publishing country	United States
Document type	Comment ; Journal Article
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.1129761
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Article ; Online: The fusion loops and membrane proximal region of Epstein-Barr virus glycoprotein B (gB) can function in the context of herpes simplex virus 1 gB when substituted individually but not in combination.

Zago, Anna / Connolly, Sarah A / Spear, Patricia G / Longnecker, Richard

Virus research

2012 Volume 171, Issue 1, Page(s) 227–230

Abstract: Among the herpesvirus glycoprotein B (gB) fusion proteins, the hydrophobic content of fusion loops and membrane proximal regions (MPRs) are inversely correlated with each other. We examined the functional importance of the hydrophobicity of these regions ...

Abstract	Among the herpesvirus glycoprotein B (gB) fusion proteins, the hydrophobic content of fusion loops and membrane proximal regions (MPRs) are inversely correlated with each other. We examined the functional importance of the hydrophobicity of these regions by replacing them in herpes simplex virus type 1 gB with corresponding regions from Epstein-Barr virus gB. We show that fusion activity is dependent on the structural context in which the specific loops and MPR sequences exist, rather than a simple hydrophobic relationship.
MeSH term(s)	Amino Acid Motifs ; Amino Acid Sequence ; Animals ; CHO Cells ; Cell Line ; Cricetinae ; Herpesvirus 1, Human/metabolism ; Herpesvirus 4, Human/metabolism ; Humans ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Sequence Alignment ; Viral Envelope Proteins/chemistry ; Viral Envelope Proteins/metabolism
Chemical Substances	Viral Envelope Proteins ; glycoprotein B, Simplexvirus
Language	English
Publishing date	2012-10-23
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	605780-9
ISSN	1872-7492 ; 0168-1702
ISSN (online)	1872-7492
ISSN	0168-1702
DOI	10.1016/j.virusres.2012.10.015
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Article ; Online: Insertional mutations in herpes simplex virus type 1 gL identify functional domains for association with gH and for membrane fusion.

Fan, Qing / Lin, Erick / Spear, Patricia G

Journal of virology

2009 Volume 83, Issue 22, Page(s) 11607–11615

Abstract: Glycoprotein L (gL) is one of four glycoproteins required for the entry of herpes simplex virus (HSV) into cells and for virus-induced cell fusion. This glycoprotein oligomerizes with gH to form a membrane-bound heterodimer but can be secreted when ... ...

Abstract	Glycoprotein L (gL) is one of four glycoproteins required for the entry of herpes simplex virus (HSV) into cells and for virus-induced cell fusion. This glycoprotein oligomerizes with gH to form a membrane-bound heterodimer but can be secreted when expressed without gH. Twelve unique gL linker-insertion mutants were generated to identify regions critical for gH binding and gH/gL processing and regions essential for cell fusion and viral entry. All gL mutants were detected on the cell surface in the absence of gH, suggesting incomplete cleavage of the signal peptide or the presence of a cell surface receptor for secreted gL. Coexpression with gH enhanced the levels of cell surface gL detected by antibodies for all gL mutants except those that were defective in their interactions with gH. Two insertions into a conserved region of gL abrogated the binding of gL to gH and prevented gH expression on the cell surface. Three other insertions reduced the cell surface expression of gH and/or altered the properties of gH/gL heterodimers. Altered or absent interaction of gL with gH was correlated with reduced or absent cell fusion activity and impaired complementation of virion infectivity. These results identify a conserved domain of gL that is critical for its binding to gH and two noncontiguous regions of gL, one of which contains the conserved domain, that are critical for the gH/gL complex to perform its role in membrane fusion.
MeSH term(s)	Animals ; CHO Cells ; Cricetinae ; Cricetulus ; Dimerization ; Herpesvirus 1, Human/genetics ; Mutagenesis, Insertional/genetics ; Protein Structure, Tertiary/genetics ; Viral Envelope Proteins/genetics ; Viral Envelope Proteins/physiology ; Virus Integration/genetics ; Virus Internalization
Chemical Substances	Viral Envelope Proteins ; glycoprotein H, herpes simplex virus type 1 ; glycoprotein L, Human herpesvirus 1
Language	English
Publishing date	2009-09-02
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.01369-09
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Article: Herpesvirus entry: an update.

Spear, Patricia G / Longnecker, Richard

Journal of virology

2003 Volume 77, Issue 19, Page(s) 10179–10185

MeSH term(s)	Animals ; Herpesviridae/physiology ; Herpesvirus 4, Human/physiology ; Herpesvirus 8, Human/physiology ; Humans ; Membrane Fusion ; Receptors, Virus/physiology ; Simplexvirus/physiology ; Viral Envelope Proteins/chemistry ; Viral Envelope Proteins/metabolism
Chemical Substances	Receptors, Virus ; Viral Envelope Proteins ; glycoprotein D, Human herpesvirus 1 ; glycoprotein D-herpes simplex virus type 2
Language	English
Publishing date	2003-07-30
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.77.19.10179-10185.2003
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Article: Random mutagenesis of the gene encoding a viral ligand for multiple cell entry receptors to obtain viral mutants altered for receptor usage.

Yoon, Miri / Spear, Patricia G

Proceedings of the National Academy of Sciences of the United States of America

2004 Volume 101, Issue 49, Page(s) 17252–17257

Abstract: Herpes simplex virus type 1 (HSV-1) can enter cells expressing any one of multiple entry receptors, including the herpesvirus entry mediator (HVEM), nectin-1, and sites in heparan sulfate generated by specific 3-O-sulfotransferases. The viral ligand for ... ...

Abstract	Herpes simplex virus type 1 (HSV-1) can enter cells expressing any one of multiple entry receptors, including the herpesvirus entry mediator (HVEM), nectin-1, and sites in heparan sulfate generated by specific 3-O-sulfotransferases. The viral ligand for these receptors is glycoprotein D (gD). To define structural requirements for functional interactions of gD with its receptors and to obtain viral mutants altered for receptor usage, we generated a library of HSV-1 mutants with random mutations in the gD gene. Viral isolates selected on a monkey cell line (Vero) were screened for the loss of ability to infect cells expressing each of the HSV-1 receptors. The 10 HSV-1 mutants obtained had 12 mutations in gD, affecting 11 amino acids. All mutations reduced or abrogated viral entry through HVEM and 3-O-sulfated heparan sulfate, indicating that similar features of gD are critical for functional interactions with both these receptors. None of the mutations reduced viral entry through nectin-1, whereas a subset of the mutations conferred ability to use nectin-2 as an entry receptor. These and other results show that features of gD, including conformation of the N terminus, critical for functional interactions with HVEM/3-O-sulfated heparan sulfate, differ from those critical for interactions with nectin-1.
MeSH term(s)	Animals ; Binding Sites ; Chlorocebus aethiops ; Heparin/analogs & derivatives ; Heparin/chemistry ; Herpesvirus 1, Human/genetics ; Herpesvirus 1, Human/pathogenicity ; Mutagenesis ; Mutation, Missense ; Peptide Library ; Protein Binding ; Protein Conformation ; Proteoglycans/chemistry ; Receptors, Tumor Necrosis Factor/chemistry ; Receptors, Tumor Necrosis Factor, Member 14 ; Receptors, Virus/chemistry ; Vero Cells ; Viral Envelope Proteins/chemistry ; Viral Envelope Proteins/genetics ; Viral Envelope Proteins/physiology
Chemical Substances	Peptide Library ; Proteoglycans ; Receptors, Tumor Necrosis Factor ; Receptors, Tumor Necrosis Factor, Member 14 ; Receptors, Virus ; TNFRSF14 protein, human ; Viral Envelope Proteins ; glycoprotein D, Human herpesvirus 1 ; heparin proteoglycan ; Heparin (9005-49-6)
Language	English
Publishing date	2004-11-22
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.0407892101
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