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Glc

1,4. b. Gal. NTHi 375 LPS structure. lgtF. opsX. lic1**. P..P. Etn. 4. 1,4. 1,5. 6. b. a. P. C. Glc. Hep. Kdo. LipidA. 1,3. a. lpt6. P. Etn. Hep. lgtC**. 6. 1,2. a. 1,4. 1,2. a. b. Gal. Glc. Hep. 4. 2,3. a. Neu5Ac. lic2A**. lpsA. ** : phase variable gene.

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Glc

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  1. 1,4 b Gal NTHi 375 LPS structure lgtF opsX lic1** P..P Etn 4 1,4 1,5 6 b a P C Glc Hep Kdo LipidA 1,3 a lpt6 P Etn Hep lgtC** 6 1,2 a 1,4 1,2 a b Gal Glc Hep 4 2,3 a Neu5Ac lic2A** lpsA **: phase variable gene

  2. 375 glycosyltransferases mutants: opsX - lpsA- lic2A- (CAAT) lgtC - (GACA) lgtF - 375 phosphoethanolamine mutant: 375 phosphocholine mutant: lpt6 - lic1 - (CAAT)

  3. Glycobiology, 2001, Vol. 11, No. 11: 957-967 Genetic basis for expression of the major globotetraose-containing lipopolysaccharide from H. influenzae strain Rd (RM118) Derek W. Hood, Andrew D. Cox, Warren W. Wakarchuk, Melissa Schur, Elke K.H. Schweda, Shannon L. Walsh, Mary E. Deadman, Adele Martin, E. Richard Moxon and James C. Richards The electrophoretic gel-migration patterns after T–SDS–PAGE of LPS purified from RM118 wild type and strains mutated in putative glycosyltransferase genes. RM118 corresponds to the wild-type strain, and the isogenic mutants are listed by the relevant LPS gene.

  4. The 375hmg+ strain is 375 transformed with the DNA from the hmg locus. It does produce a higher molecular weight LPS band on gels and gains reactivity to mAb LLA5 but the detailed structure has not been characterised. This strain should present an additional sialylation site.

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