Anaplasma phagocytophilum Asp14 is an invasin that interacts with mammalian host cells via its C terminus to facilitate infection

Infection and Immunity

Volumn 81, Issue 1, 2013, Pages 65-79

  Kahlon, Amandeep ^a   Ojogun, Nore ^a   Ragland, Stephanie A ^a,d   Seidman, David ^a   Troese, Matthew J ^a,e   Ottens, Andrew K ^a   Mastronunzio, Juliana E ^b   Truchan, Hilary K ^a   Walker, Naomi J ^c   Borjesson, Dori L ^c   Fikrig, Erol ^b   Carlyon, Jason A ^a  

^a VIRGINIA COMMONWEALTH UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d UNIVERSITY OF VIRGINIA   (United States)

^e MB Research Laboratories   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ANTISERUM; ASP14 PROTEIN; AVIDIN; BACTERIAL PROTEIN; CELL SURFACE PROTEIN; GLUTATHIONE TRANSFERASE; INVASIN; MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN A; P SELECTIN GLYCOPROTEIN LIGAND 1; PROTEOME; UNCLASSIFIED DRUG;

ANAPLASMA PHAGOCYTOPHILUM; ARTICLE; BACTERIAL TRANSMISSION; BINDING AFFINITY; BIOTINYLATION; CARBOXY TERMINAL SEQUENCE; CELL ADHESION; CELL INVASION; CELL SURFACE; CONTROLLED STUDY; EHRLICHIA; GENE EXPRESSION PROFILING; GENE LOCUS; GENETIC TRANSCRIPTION; HOST CELL; HUMAN; HUMAN CELL; HUMAN GRANULOCYTIC ANAPLASMOSIS; MAMMAL CELL; MASS SPECTROMETRY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN TARGETING; UPREGULATION;

AMINO ACID SEQUENCE; ANAPLASMA PHAGOCYTOPHILUM; ANIMALS; BACTERIAL OUTER MEMBRANE PROTEINS; BINDING SITES; CELL ADHESION; CELL LINE, TUMOR; EHRLICHIA; EHRLICHIOSIS; GENE EXPRESSION REGULATION, BACTERIAL; GLUTATHIONE TRANSFERASE; HL-60 CELLS; HUMANS; MEMBRANE GLYCOPROTEINS; MEMBRANE PROTEINS; MICE; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEOME; SEQUENCE ANALYSIS, PROTEIN; TRANSCRIPTION, GENETIC; UP-REGULATION;

EID: 84871864040     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00932-12     Document Type: Article

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