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Article ; Online: Scylla, Charybdis, and navigating antimicrobial action in the neutrophil phagosome.

Nauseef, William M

2022 Volume 112, Issue 4, Page(s) 587–589

Abstract: The text extracted from the initial paragraph of a paper coauthored by Zanvil Cohn, one of the pioneers in the study of leukocyte biology, highlights two phenomena that stimulated investigations of innate immunity in the middle of the last century, ... ...

Abstract	The text extracted from the initial paragraph of a paper coauthored by Zanvil Cohn, one of the pioneers in the study of leukocyte biology, highlights two phenomena that stimulated investigations of innate immunity in the middle of the last century, namely phagocytosis and intracellular antimicrobial activity. Although many features of phagocytosis have been characterized since that time, fundamental aspects of the antimicrobial action of neutrophils remain unknown. The report by Ashby et al. provides a refined and nuanced look at the interface between an ingested microbe, Staphylococcus aureus, and HOCl generated by the myeloperoxidase (MPO)-H
MeSH term(s)	Anti-Bacterial Agents/pharmacology ; Chlorides/pharmacology ; Hypochlorous Acid ; Neutrophils ; Peroxidase ; Phagocytosis ; Phagosomes
Chemical Substances	Anti-Bacterial Agents ; Chlorides ; Hypochlorous Acid (712K4CDC10) ; Peroxidase (EC 1.11.1.7)
Language	English
Publishing date	2022-08-04
Publishing country	England
Document type	Editorial
ZDB-ID	605722-6
ISSN	1938-3673 ; 0741-5400
ISSN (online)	1938-3673
ISSN	0741-5400
DOI	10.1002/JLB.4CE0422-232R
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Article ; Online: Human neutrophils

Nauseef, William M

Immunological reviews

2022 Volume 314, Issue 1, Page(s) 442–456

Abstract: Human and murine neutrophils differ with respect to representation in blood, receptors, nuclear morphology, signaling pathways, granule proteins, NADPH oxidase regulation, magnitude of oxidant and hypochlorous acid production, and their repertoire of ... ...

Abstract	Human and murine neutrophils differ with respect to representation in blood, receptors, nuclear morphology, signaling pathways, granule proteins, NADPH oxidase regulation, magnitude of oxidant and hypochlorous acid production, and their repertoire of secreted molecules. These differences often matter and can undermine extrapolations from murine studies to clinical care, as illustrated by several failed therapeutic interventions based on mouse models. Likewise, coevolution of host and pathogen undercuts fidelity of murine models of neutrophil-predominant human infections. However, murine systems that accurately model the human condition can yield insights into human biology difficult to obtain otherwise. The challenge for investigators who employ murine systems is to distinguish models from pretenders and to know when the mouse provides biologically accurate insights. Testing with human neutrophils observations made in murine systems would provide a safeguard but is not always possible. At a minimum, studies that use exclusively murine neutrophils should have accurate titles supported by data and restrict conclusions to murine neutrophils and not encompass all neutrophils. For now, the integration of evidence from studies of neutrophil biology performed using valid murine models coupled with testing in vitro of human neutrophils combines the best of both approaches to elucidate the mysteries of human neutrophil biology.
MeSH term(s)	Humans ; Mice ; Animals ; Neutrophils ; NADPH Oxidases/metabolism ; Signal Transduction
Chemical Substances	NADPH Oxidases (EC 1.6.3.-)
Language	English
Publishing date	2022-11-15
Publishing country	England
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural
ZDB-ID	391796-4
ISSN	1600-065X ; 0105-2896
ISSN (online)	1600-065X
ISSN	0105-2896
DOI	10.1111/imr.13154
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Article ; Online: Neutrophils and their friends.

Cassatella, Marco A / Nauseef, William M

Immunological reviews

2023 Volume 314, Issue 1, Page(s) 6–12

MeSH term(s)	Humans ; Neutrophils ; Friends
Language	English
Publishing date	2023-01-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	391796-4
ISSN	1600-065X ; 0105-2896
ISSN (online)	1600-065X
ISSN	0105-2896
DOI	10.1111/imr.13188
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Article ; Online: Human neutrophils ≠ murine neutrophils: Does it matter?

Nauseef, William M.

Immunological Reviews 2023 Mar., v. 314, no. 1, p. 442-456

2023 , Page(s) 442–456

Abstract	Human and murine neutrophils differ with respect to representation in blood, receptors, nuclear morphology, signaling pathways, granule proteins, NADPH oxidase regulation, magnitude of oxidant and hypochlorous acid production, and their repertoire of secreted molecules. These differences often matter and can undermine extrapolations from murine studies to clinical care, as illustrated by several failed therapeutic interventions based on mouse models. Likewise, coevolution of host and pathogen undercuts fidelity of murine models of neutrophil‐predominant human infections. However, murine systems that accurately model the human condition can yield insights into human biology difficult to obtain otherwise. The challenge for investigators who employ murine systems is to distinguish models from pretenders and to know when the mouse provides biologically accurate insights. Testing with human neutrophils observations made in murine systems would provide a safeguard but is not always possible. At a minimum, studies that use exclusively murine neutrophils should have accurate titles supported by data and restrict conclusions to murine neutrophils and not encompass all neutrophils. For now, the integration of evidence from studies of neutrophil biology performed using valid murine models coupled with testing in vitro of human neutrophils combines the best of both approaches to elucidate the mysteries of human neutrophil biology.
Keywords	NAD(P)H oxidase (H2O2-forming) ; coevolution ; humans ; mice ; neutrophils ; oxidants ; pathogens ; therapeutics
Language	English
Dates of publication	2023-03
Size	p. 442-456.
Publishing place	John Wiley & Sons, Inc
Document type	Article ; Online
ZDB-ID	391796-4
ISSN	1600-065X ; 0105-2896
ISSN (online)	1600-065X
ISSN	0105-2896
DOI	10.1111/imr.13154
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Article ; Online: Neutrophil dysfunction in the pathogenesis of cystic fibrosis.

Wang, Guoshun / Nauseef, William M

Blood

2022 Volume 139, Issue 17, Page(s) 2622–2631

Abstract: Polymorphonuclear neutrophils (PMNs) figure prominently in host defense against infection and in noninfectious inflammation. Mobilized early in an inflammatory response, PMNs mediate immediate cellular defense against microbes and orchestrate events that ...

Abstract	Polymorphonuclear neutrophils (PMNs) figure prominently in host defense against infection and in noninfectious inflammation. Mobilized early in an inflammatory response, PMNs mediate immediate cellular defense against microbes and orchestrate events that culminate in cessation of inflammation and restoration of homeostasis. Failure to terminate the inflammatory response and its causes can fuel exuberant inflammation characteristic of many human diseases, including cystic fibrosis (CF), an autosomal recessive genetic disease caused by mutations in the CF transmembrane conductance regulator. CF affects multiple end organs, with persistent bacterial infection and chronic neutrophilic inflammation in airways predominating the clinical picture. To match the diverse microbial challenges that they may encounter, PMNs possess a variety of antimicrobial systems to slow or kill invading microorganisms confined in their phagosomes. Prominent among PMN defense systems is their ability to generate hypochlorous acid, a potent microbicide, by reacting oxidants generated by the NADPH oxidase with myeloperoxidase (MPO) released from azurophilic granules in the presence of chloride (Cl-). Products of the MPO-H2O2-Cl system oxidize susceptible biomolecules and support robust antimicrobial action against many, but not all, potential human pathogens. Underscoring that the MPO-H2O2-Cl system is integral to optimal host defense and proper regulation of inflammation, individuals with defects in any component of this system, as seen in chronic granulomatous disease or MPO deficiency, incur increased rates or severity of infection and signs of dysregulated inflammatory responses. We focus attention in this review on the molecular basis for and the clinical consequences of defects in the MPO-H2O2-Cl system because of the compromised Cl transport seen in CF. We will discuss first how the MPO-H2O2-Cl system in healthy PMNs participates in host defense and resolution of inflammation and then review how a defective MPO-H2O2-Cl system contributes to the increased susceptibility to infection and dysregulated inflammation associated with the clinical manifestations of CF.
MeSH term(s)	Chlorides ; Cystic Fibrosis ; Humans ; Hydrogen Peroxide ; Hypochlorous Acid ; Inflammation ; Leukocyte Disorders ; Neutrophils/microbiology ; Peroxidase
Chemical Substances	Chlorides ; Hypochlorous Acid (712K4CDC10) ; Hydrogen Peroxide (BBX060AN9V) ; Peroxidase (EC 1.11.1.7)
Language	English
Publishing date	2022-02-25
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural
ZDB-ID	80069-7
ISSN	1528-0020 ; 0006-4971
ISSN (online)	1528-0020
ISSN	0006-4971
DOI	10.1182/blood.2021014699
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Article ; Online: The phagocyte NOX2 NADPH oxidase in microbial killing and cell signaling.

Nauseef, William M

Current opinion in immunology

2019 Volume 60, Page(s) 130–140

Abstract: The phagocyte NADPH oxidase possesses a transmembrane electron transferase comprised of gp91phox (aka NOX2) and p22phox and two multicomponent cytosolic complexes, which in stimulated phagocytes translocate to assemble a functional enzyme complex at ... ...

Abstract	The phagocyte NADPH oxidase possesses a transmembrane electron transferase comprised of gp91phox (aka NOX2) and p22phox and two multicomponent cytosolic complexes, which in stimulated phagocytes translocate to assemble a functional enzyme complex at plasma or phagosomal membranes. The NOX2-centered NADPH oxidase shuttles electrons from cytoplasmic NADPH to molecular oxygen in phagosomes or the extracellular space to produce oxidants that support optimal antimicrobial activity by phagocytes. Additionally, NOX2-generated oxidants have been implicated in both autocrine and paracrine signaling in a variety of biological contexts. However, when interpreting experimental results, investigators must recognize the complexity inherent in the biochemistry of oxidant-mediated attack of microbial targets and the technical limitations of the probes currently used to detect intracellular oxidants.
MeSH term(s)	Animals ; Granulomatous Disease, Chronic/etiology ; Granulomatous Disease, Chronic/metabolism ; Granulomatous Disease, Chronic/pathology ; Humans ; Hydrogen Peroxide/metabolism ; NADPH Oxidase 2/metabolism ; Neutrophils/metabolism ; Oxidants/metabolism ; Oxidation-Reduction ; Phagocytes/immunology ; Phagocytes/metabolism ; Phagocytosis ; Phagosomes/metabolism ; Signal Transduction
Chemical Substances	Oxidants ; Hydrogen Peroxide (BBX060AN9V) ; NADPH Oxidase 2 (EC 1.6.3.-)
Language	English
Publishing date	2019-07-11
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
ZDB-ID	1035767-1
ISSN	1879-0372 ; 0952-7915
ISSN (online)	1879-0372
ISSN	0952-7915
DOI	10.1016/j.coi.2019.05.006
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Article ; Online: Biosynthesis of human myeloperoxidase.

Nauseef, William M

Archives of biochemistry and biophysics

2018 Volume 642, Page(s) 1–9

Abstract: Members of Chordata peroxidase subfamily [1] expressed in mammals, including myeloperoxidase (MPO), eosinophil peroxidase (EPO), lactoperoxidase (LPO), and thyroid peroxidase (TPO), express conserved motifs around the heme prosthetic group essential for ... ...

Abstract	Members of Chordata peroxidase subfamily [1] expressed in mammals, including myeloperoxidase (MPO), eosinophil peroxidase (EPO), lactoperoxidase (LPO), and thyroid peroxidase (TPO), express conserved motifs around the heme prosthetic group essential for their activity, a calcium-binding site, and at least two covalent bonds linking the heme group to the protein backbone. Although most studies of the biosynthesis of these peroxidases have focused on MPO, many of the features described occur during biosynthesis of other members of the protein subfamily. Whereas MPO biosynthesis includes events typical for proteins generated in the secretory pathway, the importance and consequences of heme insertion are events uniquely associated with peroxidases. This Review summarizes decades of work elucidating specific steps in the biosynthetic pathway of human MPO. Discussion includes cotranslational glycosylation and subsequent modifications of the N-linked carbohydrate sidechains, contributions by molecular chaperones in the endoplasmic reticulum, cleavage of the propeptide from proMPO, and proteolytic processing of protomers and dimerization to yield mature MPO. Parallels between the biosynthesis of MPO and TPO as well as the impact of inherited mutations in the MPO gene on normal biosynthesis will be summarized. Lastly, specific gaps in our knowledge revealed by this review of our current understanding will be highlighted.
MeSH term(s)	Binding Sites ; Calcium/metabolism ; Dimerization ; Endoplasmic Reticulum/enzymology ; Endoplasmic Reticulum/metabolism ; Eosinophil Peroxidase/biosynthesis ; Glycosylation ; Heme/metabolism ; Humans ; Iodide Peroxidase/biosynthesis ; Lactoperoxidase/biosynthesis ; Peroxidase/biosynthesis ; Peroxidase/genetics ; Peroxidase/metabolism ; Proteolysis
Chemical Substances	Heme (42VZT0U6YR) ; Eosinophil Peroxidase (EC 1.11.1.-) ; Lactoperoxidase (EC 1.11.1.-) ; Peroxidase (EC 1.11.1.7) ; Iodide Peroxidase (EC 1.11.1.8) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2018-02-03
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2018.02.001
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Article ; Online: In the beginning and at the end: calreticulin.

Nauseef, William M

Blood

2016 Volume 127, Issue 25, Page(s) 3113–3114

MeSH term(s)	Calcium-Binding Proteins ; Calreticulin ; Humans ; Ribonucleoproteins
Chemical Substances	Calcium-Binding Proteins ; Calreticulin ; Ribonucleoproteins
Language	English
Publishing date	2016-06-23
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	80069-7
ISSN	1528-0020 ; 0006-4971
ISSN (online)	1528-0020
ISSN	0006-4971
DOI	10.1182/blood-2016-04-708198
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Article ; Online: Neutrophils, from cradle to grave and beyond.

Nauseef, William M

Immunological reviews

2016 Volume 273, Issue 1, Page(s) 5–10

MeSH term(s)	Animals ; Cell Communication ; Cell Degranulation ; Cell Differentiation ; Gene Expression Regulation ; Humans ; Immunity, Innate ; Infections/immunology ; Inflammation/immunology ; Interleukin-8/metabolism ; Leukocyte Elastase/metabolism ; MicroRNAs/genetics ; NADPH Oxidases/metabolism ; Neutrophils/immunology ; Neutrophils/microbiology ; Transendothelial and Transepithelial Migration
Chemical Substances	Interleukin-8 ; MicroRNAs ; NADPH Oxidases (EC 1.6.3.-) ; Leukocyte Elastase (EC 3.4.21.37)
Language	English
Publishing date	2016-08-24
Publishing country	England
Document type	Introductory Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	391796-4
ISSN	1600-065X ; 0105-2896
ISSN (online)	1600-065X
ISSN	0105-2896
DOI	10.1111/imr.12463
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Article ; Online: Isolation of Human Neutrophils from Venous Blood.

Kremserova, Silvie / Nauseef, William M

Methods in molecular biology (Clifton, N.J.)

2019 Volume 2087, Page(s) 33–42

Abstract: Venous blood provides a ready source of large numbers of unstimulated granulocytes and mononuclear cells. Exploiting the differences in the relative densities of the leukocytes circulating in venous blood, one can separate leukocytes from erythrocytes as ...

Abstract	Venous blood provides a ready source of large numbers of unstimulated granulocytes and mononuclear cells. Exploiting the differences in the relative densities of the leukocytes circulating in venous blood, one can separate leukocytes from erythrocytes as well as isolate the individual leukocyte populations in high purity for use in ex vivo studies. For selected functional studies, such as transcriptional analysis or cytokine quantitation, addition of an immunomagnetic negative selection step to the standard isolation protocol can yield highly purified human neutrophils.
MeSH term(s)	Cell Separation/methods ; Centrifugation, Density Gradient/methods ; Dextrans ; Ficoll ; Humans ; Leukocyte Count ; Neutrophils/cytology ; Neutrophils/metabolism
Chemical Substances	Dextrans ; Ficoll (25702-74-3)
Language	English
Publishing date	2019-11-14
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-0154-9_3
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