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1.
One Health ; 11: 100192, 2021 Jun.
Article in English | MEDLINE | ID: mdl-33169106

ABSTRACT

In a survey of household cats and dogs of laboratory-confirmed COVID-19 patients, we found a high seroprevalence of SARS-CoV-2 antibodies, ranging from 21% to 53%, depending on the positivity criteria chosen. Seropositivity was significantly greater among pets from COVID-19+ households compared to those with owners of unknown status. Our results highlight the potential role of pets in the spread of the epidemic.

2.
Cell Rep ; 23(9): 2568-2581, 2018 05 29.
Article in English | MEDLINE | ID: mdl-29847789

ABSTRACT

Human high-affinity antibodies to pathogens often recognize unrelated ligands. The molecular origin and the role of this polyreactivity are largely unknown. Here, we report that HIV-1 broadly neutralizing antibodies (bNAbs) are frequently polyreactive, cross-reacting with non-HIV-1 molecules, including self-antigens. Mutating bNAb genes to increase HIV-1 binding and neutralization also results in de novo polyreactivity. Unliganded paratopes of polyreactive bNAbs with improved HIV-1 neutralization exhibit a conformational flexibility, which contributes to enhanced affinity of bNAbs to various HIV-1 envelope glycoproteins and non-HIV antigens. Binding adaptation of polyreactive bNAbs to the divergent ligands mainly involves hydrophophic interactions. Plasticity of bNAbs' paratopes may, therefore, facilitate accommodating divergent viral variants, but it simultaneously triggers promiscuous binding to non-HIV-1 antigens. Thus, a certain level of polyreactivity can be a mark of adaptable antibodies displaying optimal pathogens' recognition.


Subject(s)
Antibodies, Neutralizing/chemistry , Antibodies, Neutralizing/immunology , HIV Antibodies/chemistry , HIV Antibodies/immunology , HIV-1/immunology , Autoantigens/immunology , Binding Sites, Antibody , Cross Reactions/immunology , HIV Antigens/immunology , Humans , Hydrophobic and Hydrophilic Interactions , Immunoglobulin Fab Fragments/immunology , Neutralization Tests , Protein Conformation , Thermodynamics , env Gene Products, Human Immunodeficiency Virus/metabolism
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