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Host-pathogen interactions in Streptococcus pyogenes infections, with special reference to puerperal fever and a comment on vaccine development.

Streptococcus pyogenes (group A streptococcus) causes a variety of diseases, including acute pharyngitis, impetigo, rheumatic fever and the streptococcal toxic shock syndrome. Moreover, S. pyogenes was responsible for the classical example of a nosocomial infection, the epidemics of puerperal fever (childbed fever) that caused the death of numerous women in earlier centuries. The most extensively

Evolutionary and functional studies of protein H: a surface molecule of Streptococcus pyogenes

Popular Abstract in Swedish Protein H - ett bakteriellt ytprotein med förmåga att binda till olika proteiner hos människa Bakgrund I vårt dagliga liv omges vi av bakterier av många olika slag. Flertalet av dessa är normalt ofarliga och många utgör den så kallade normalfloran hos människa. En del bakterier kan under vissa förhållanden ge upphov till infektion och sjukdom, men för att åstadkomma d

Inga Persson

Professor emerita Contact details Email: inga [dot] persson [at] nek [dot] lu [dot] se Phone: +46 46 222 95 47Organisation Department of Economics Room number: EC1:267 Service point: 10 WebpageInga Perssons profile in Lund University research portalOther affiliations Professor emerita Centre for Economic Demography Publications Displaying of publications. Sorted by year, then title. Filter by type

https://www.lusem.lu.se/inga-persson - 2026-05-14

Receptor for IgA in group A streptococci : cloning of the gene and characterization of the protein expressed in Escherichia coli

The gene for an IgA-binding protein from a group A streptococcal strain was cloned and expressed in Escherichia coli. The IgA-binding protein, called protein Arp, was purified on IgA-Sepharose, allowing complete purification in a single step. Analysis of protein Arp by Western immunoblotting demonstrated a major IgA-binding band, with an apparent molecular weight of 42 kD. The purified protein was

A highly sensitive bead-based flow cytometric competitive binding assay to detect SARS-CoV-2 neutralizing antibody activity

Accurate detection of SARS-CoV-2 neutralizing antibody (nAb) is critical for assessing the immunity levels after virus infection or vaccination. As fast, cost-effective alternatives to viral infection-based assays, competitive binding (CB) assays were developed to quantitate nAb by monitoring the ability of sera to inhibit the binding of viral spike (S) protein to the angiotensin converting enzyme