Surface Glycopolymers Are Crucial for In Vitro Anti-Wall Teichoic Acid IgG-Mediated Complement Activation and Opsonophagocytosis of Staphylococcus aureus.
The cell envelopes of many Gram-positive bacteria contain wall teichoic acids (WTAs). Staphylococcus aureus WTAs are composed of ribitol phosphate (RboP) or glycerol phosphate (GroP) backbones substituted with D-alanine and N-acetyl-D-glucosamine (GlcNAc) or N-acetyl-D-galactosamine (GalNAc). Two WTA glycosyltransferases, TarM and TarS, are responsible for modifying the RboP WTA with α-GlcNAc and β-GlcNAc, respectively. We recently reported that purified human serum anti-WTA IgG specifically recognizes β-GlcNAc of the staphylococcal RboP WTA and then facilitates complement C3 deposition and opsonophagocytosis of S. aureus laboratory strains. This prompted us to examine whether anti-WTA IgG can induce C3 deposition on a diverse set of clinical S. aureus isolates. To this end, we compared anti-WTA IgG-mediated C3 deposition and opsonophagocytosis abilities using 13 different staphylococcal strains. Of note, the majority of S. aureus strains tested was recognized by anti-WTA IgG, resulting in C3 deposition and opsonophagocytosis. A minority of strains was not recognized by anti-WTA IgG, which correlated with either extensive capsule production or an alteration in the WTA glycosylation pattern. Our results demonstrate that the presence of WTAs with TarS-mediated glycosylation with β-GlcNAc in clinically isolated S. aureus strains is an important factor for induction of anti-WTA IgG-mediated C3 deposition and opsonophagocytosis.
National Research Laboratory of Defense Proteins, College of Pharmacy, Pusan National University, Geumjeong Gu, Busan, South Korea.
Jong-Ho
JH
Lee
National Research Laboratory of Defense Proteins, College of Pharmacy, Pusan National University, Geumjeong Gu, Busan, South Korea.
Na-Hyang
NH
Kim
Cellular and Molecular Microbiology Division, Interfaculty Institute of Microbiology and Infection Medicine, University of Tübingen, and German Center for Infection Research, Partner Site Tübingen, Tübingen, Germany.
Volker
V
Winstel
Faculty of Pharmaceutical Sciences, Nagasaki International University, Sasebo, Nagasaki, Japan.
Kenji
K
Kurokawa
Microbiology & Infection Control, Statens Serum Institut, Copenhagen, Denmark.
Jesper
J
Larsen
National Research Laboratory of Defense Proteins, College of Pharmacy, Pusan National University, Geumjeong Gu, Busan, South Korea.
Jang-Hyun
JH
An
National Research Laboratory of Defense Proteins, College of Pharmacy, Pusan National University, Geumjeong Gu, Busan, South Korea.
Adnan
A
Khan
National Research Laboratory of Defense Proteins, College of Pharmacy, Pusan National University, Geumjeong Gu, Busan, South Korea.
Min-Young
MY
Seong
National Research Laboratory of Defense Proteins, College of Pharmacy, Pusan National University, Geumjeong Gu, Busan, South Korea.
Min Ja
MJ
Lee
Microbiology & Infection Control, Statens Serum Institut, Copenhagen, Denmark.
Paal Skytt
PS
Andersen
Cellular and Molecular Microbiology Division, Interfaculty Institute of Microbiology and Infection Medicine, University of Tübingen, and German Center for Infection Research, Partner Site Tübingen, Tübingen, Germany.
Andreas
A
Peschel
National Research Laboratory of Defense Proteins, College of Pharmacy, Pusan National University, Geumjeong Gu, Busan, South Korea brlee@pusan.ac.kr.
Bok Luel
BL
Lee
D001426:Bacterial Proteins / Q000378:metabolism; D002473:Cell Wall / Q000276:immunology*; D003167:Complement Activation; D003176:Complement C3 / Q000276:immunology*; D016695:Glycosyltransferases / Q000378:metabolism; D006801:Humans; D007074:Immunoglobulin G / Q000276:immunology*; D010587:Phagocytosis; D013203:Staphylococcal Infections / Q000276:immunology* / Q000382:microbiology; D013211:Staphylococcus aureus / Q000201:enzymology / Q000235:genetics / Q000276:immunology*; D013682:Teichoic Acids / Q000276:immunology*
D001426:Bacterial Proteins; D003176:Complement C3; D007074:Immunoglobulin G; D013682:Teichoic Acids; D016695:Glycosyltransferases