Natural immunity to bacterial infections: the relation of complement to heat-labile opsonins.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 63 ·No. 4 ·1969-08-00 ·Pages 1151-6

Smith MR, Shin HS, Wood WB

Abstract

Heat-labile opsonins to pneumococci in normal mammalian sera, unlike antibodies, fail to interact with the bacteria at 0 degrees C and require Ca(++) and/or Mg(++). They are readily removed from serum by antigen-antibody complexes that fix complement (C) and are inhibited by reagents that inactivate various C components. The principal heat-labile opsonin to pneumococci is activated C3 (C3(b)), but a slight enhancing effect is exerted by one or more of the late-reacting components of the hemolytic complement system (C5-C9). Since heat-labile opsonins are immunologically polyspecific, they presumably play a broad protective role in the early (preantibody) phase of acute bacterial infections.

MeSH Terms

Animals Complement System Proteins/pharmacology Guinea Pigs Hot Temperature Opsonin Proteins Phagocytosis Pneumococcal Infections/immunology Rats Streptococcus pneumoniae/immunology

Chemicals

Opsonin Proteins Complement System Proteins

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Smith M R

Shin H S

Wood W B

References (13)

13 references, click to expand

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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.63.4.1151

Published

1969-08-00

Pages

1151-6

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC223442

Subset

External Links

PubMed source DOI: 10.1073/pnas.63.4.1151 PMC Full Text View journal details

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Natural immunity to bacterial infections: the relation of complement to heat-labile opsonins.

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